Peptide mutant of human ERAB or HADH2, its X-ray crystal structure, and materials and method for identification of inhibitors thereof

ABSTRACT

The identification, isolation and modification of human ERAB or HADH2 is described. A crystal structure of ERAB or HADH2 is described which may be used in the discovery, identification and characterization of inhibitors or modulators of ERAB or HADH2. This structure provides a three-dimensional description of binding sites of ERAB or HADH2 for structure-based design of inhibitors or modulators thereof as therapeutic agents, for example in the treatment of Alzheimer&#39;s disease).

CROSS REFERENCES OF RELATED APPLICATIONS

[0001] This application claims the benefit of U.S. Provisional Application, Ser. No. 60/226123, filed Aug. 18, 2000.

TECHNICAL FIELD OF THE INVENTION

[0002] The present invention relates to the three-dimensional crystal structure of human ERAB or HADH2 with NAD⁺ cofactor and its use in the design and development of inhibitors thereof.

BACKGROUND OF THE INVENTION

[0003] Endoplasmic reticulum-associated amyloid β-peptide-binding protein (ERAB), a member of the short-chain dehydrogenase/reductase (SDR) family of enzymes, has been implicated in the development of Alzheimer's disease (AD). As the name suggests, ERAB, also known as L-3-hydroxyacyl-CoA dehydrogenase Type II (HADH2), is a dehydrogenase enzyme capable of binding amyloid-β (Aβ) peptide. Inhibition of ERAB or HADH2 finds therapeutic utility in the treatment of AD and research and diagnostic utility in the delineation of the role of the enzyme in both normal cellular function and in AD pathogenesis.

[0004] AD is a progressive neurodegenerative disease of the brain resulting in diminished cognitive abilities, dementia, and ultimately death. A strong link has been established between the development of AD and the accumulation of Aβ in the brain [Storey et al., Neuropathology And Applied Neurobiology, Vol. 25, pp. 81-97 (1999); Selkoe, Annual Review of Neuroscience, Vol. 17, pp. 489-517 (1994); Small et al., J. Neurochemistry, Vol. 73, pp. 443-9 (1999)]. Aβ is a proteolytic fragment of the integral membrane glycoprotein, amyloid-β precursor protein (APP) [Kang et al., Nature, Vol. 325, pp. 733-736 (1987)]. Aβ is also the principal component of the extracellular plaques that are diagnostic of AD and species of the peptide have been shown to be engaged by intracellular targets [Yan et al., Nature, Vol. 389, pp. 689-95 (1997)]. Although aggregated Aβ appears to be toxic to neuronal cells in culture, the mechanisms of Aβ neurotoxicity in vivo are not completely understood.

[0005] Aβ accumulates both inside and outside nerve cells [Wilson et al., Journal of Neuropathology And Experimental Neurology, Vol. 58, pp. 787-94 (1999)]. There is evidence that the interaction of Aβ with intracellular proteins could lead to cytotoxic events prior to the formation of extracellular plaques. ERAB or HADH2, an intracellular protein, has been found to bind Aβ in the yeast two-hybrid system [Yan et al., Nature, Vol. 389, pp. 689-95 (1997)]. HADH2, a protein identical to ERAB, has been independently identified as an L-3-hydroxyacyl-CoA dehydrogenase with an apparent role in the mitochondrial fatty acid β-oxidation pathway [He et al., Journal of Biochemistry, Vol. 273. No. 17, pp. 10741-10746 (1998)].

[0006] ERAB or HADH2 is reported to be an NAD⁺ dependent dehydrogenase which catalyzes the reversible oxidation of L-3-hydroxyacyl-CoA. The human short chain L-3-hydroxyacyl-CoA dehydrogenase gene is organized into six exons and five introns and maps to chromosone Xp 11.2 [He et al. (1998), supra]. Sequence comparisons show that ERAB or HADH2 belongs to the SDR family of enzymes.

[0007] ERAB or HADH2 has been cloned, expressed, purified, and characterized from human brain [He et al. (1998), supra]. ERAB or HADH2 messenger RNA (mRNA) is expressed ubiquitously in normal human tissues. Its expression is highest in liver and heart but ERAB or HADH2 mRNA is also expressed in normal brain. In normal brain, ERAB or HADH2 antigen is present at low levels, being predominantly localized in neurons. However, in neurons affected in AD, ERAB or HADH2 is reported to be overexpressed relative to non-AD age-matched controls, especially near deposits of Aβ [Yan et al., Nature, Vol. 389, pp. 689-95 (1997); U.S. Pat. No. 6,268,479].

[0008] A variety of experimental evidence suggests that ERAB or HADH2 interacts with the Aβ peptide and can mediate its cytotoxic effects [Yan et al. (1997), supra]. For example, ERAB or HADH2, normally found in the endoplasmic reticulum and mitochondria, has been shown to become redistributed to the plasma membrane fraction of cells in the presence of Aβ peptide [Yan et al.(1997), supra]. Likewise, it has been shown that the cytotoxic effects of Aβ on neuroblastoma cells in cultures, can be blocked by anti-ERAB or HADH2 antibodies. Cells which overexpress ERAB or HADH2 and Aβ show elevated markers of cytotoxicity and cell stress compared to mock transfected controls; conversely, cells overexpressing catalytically inactive mutants of ERAB or HADH2 were no more sensitive than controls which overexpressed Aβ alone [Yan et al., Journal of Biochemistry, Vol. 274, pp. 2145-56 (1999)].

[0009] These observations support the theory that ERAB or HADH2 mediates the intraneuronal toxicity of Aβ by acting on inappropriate substrates, possibly generating toxic aldehydes [Yan et al., Journal of Biochemistry, Vol. 274, pp. 2145-56 (1999)]. It has also been suggested that ERAB or HADH2 could contribute to Aβ-associated pathogenesis of AD by reducing neuroprotective estrogen levels in the brain, based on the finding that the enzyme can also utilize estrogen as a substrate [Yan et al., Journal of Biochemistry, Vol. 274, pp. 2145-56 (1999); He et al., Journal of Biochemistry, Vol. 274, pp. 15014-9 (1999)]. Although the two proposed roles for ERAB or HADH2 in AD are quite distinct, enzymatic activity of the protein is a prerequisite in either case.

[0010] Several attempts have been made to elucidate the three-dimensional structure of proteins to design candidate drugs. For example, Davis et al., Prevention of Chemotherapy-Induced Alopecia in Rats by CDK Inhibitors (2001) Science 291:134-137; Zhu et al., Structural Analysis of the Lymphocyte-Specific Kinase Lck in Complex with Non-selective and Src Family selective Kinase Inhibitors (1999) Structure 7: 651-661; and Ymaguchi et al., Structural Basis for Activation of Human Lymphocyte Kinase Lck Upon Tyrosine Phosphorylation (1996) Nature 384: 484-489. U.S. Pat. Nos. 5,322,933, 5,556,778, 5,616,555, 5,872,011 and 6,020,162 disclose the three-dimensional structure of proteins, protein-ligand complex, or enzyme-cofactor complex.

SUMMARY OF THE INVENTION

[0011] The present invention relates to an isolated, purified polynucleotide that encodes a mutant ERAB or HADH2 peptide, wherein the mutant peptide is engineered to avoid cysteine oxidation. It further relates to an isolated, purified polypeptide comprising a mutant ERAB or HADH2 peptide, which is engineered to avoid cysteine oxidation. According to one embodiment, the polypeptide has an amino acid other than cysteine at one or all of positions 5, 58, and/or 214 of SEQ ID NO: 2, and particularly the polypeptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23 and functional variants thereof.

[0012] The present invention further relates to a crystalline mutant ERAB or HADH2 peptide. For one embodiment of the invention, the crystalline peptide diffracts x-rays at a resolution value of≦3 Å, and preferably≦2 Å.

[0013] The present invention further relates to a crystal of a mutant ERAB or HADH2 peptide:ligand:NAD⁺ complex comprising a mutant ERAB or HADH2 peptide:ligand:NAD⁺.

[0014] The present invention still further relates to a mutant ERAB or HADH2 peptide comprising a fold, wherein the fold comprises: a core β-sheet of seven strands sandwiched between two sets of three α-helices; and first and second insert domains, relative to other members of the short-chain dehydrogenase/reductase (SDR) family, the first insert domain forming a β hairpin that extends the surface of the ERAB or HADH2 peptide on one side of a substrate-binding cleft, and the second insert domain extending a loop between an α-helix comprising residues 123-136 and a β-sheet comprising residues 148-153 of SEQ ID NO: 2.

[0015] The present invention relates to an expression vector comprising a ploynucleotide that encodes a mutant ERAB or HADH2 peptide; transcriptional regulatory sequences functional in the host cell operably linked to the polynucleotide; and a selectable marker, as well as to a host cell stably transfected and transformed with such polynucleotide.

[0016] The present invention further relates to a method for identifying a candidate compound for its ability to interact with the human ERAB or HADH2 peptide comprising:

[0017] (a) expressing an isolated polynucleotide sequence which encodes a mutant ERAB or HADH2 peptide in a host cell capable of producing the peptide;

[0018] (b) exposing the mutant ERAB or HADH2 peptide to the candidate compound; and

[0019] (c) evaluating the interaction of the mutant ERAB or HADH2 peptide with the candidate compound.

[0020] The present invention further relates to a process of drug design for compounds which interact with ERAB or HADH2 comprising:

[0021] (a) crystallizing a mutant ERAB or HADH2 peptide;

[0022] (b) resolving the x-ray crystallography of the peptide;

[0023] (c) applying the data generated from resolving the x-ray crystallography of the peptide to a computer algorithm which generates a model of the peptide suitable for use in designing molecules that will act as agonists or antagonists to the peptide; and

[0024] (d) applying an interative process whereby various molecular structures are applied to the computer-generated model to identify potential agonists or antagonists of the peptide.

[0025] The present invention also relates to a method of assessing compounds which are agonists or antagonists of the activity of the human ERAB or HADH2 enzyme comprising:

[0026] (a) crystallizing a mutant ERAB or HADH2 peptide; obtaining crystallography coordinates for the crystallized peptide;

[0027] (b) applying the crystallography coordinates for the peptide to a computer algorithm such that the algorithm generates a model of the peptide, the model suitable for use in designing molecules that will act as agonists or antagonists to the peptide; and

[0028] (c) applying an iterative process whereby various molecular structures are applied to the computer-generated model to identify potential agonists or antagonists to the peptide.

[0029] The invention further relates to a method of identifying a compound that associates with ERAB or HADH2 comprising the step of using the structure coordinates of Table II to computationally analyze a molecular structure to evaluate a chemical compound for associating with the substrate-binding site of ERAB or HADH2 and identifying those chemical entities that associate with the substrate-binding site, wherein the step of computationally analyzing the molecular structure comprises:

[0030] (a) using a machine readable data storage medium comprising a data storage material encoded with machine readable data wherein the data comprises crystal coordinates of mutant ERAB or HADH2 peptide molecule or complex of the peptide;

[0031] (b) employing a working memory for string instructions for processing the machine readable data,

[0032] (c) using a central processor unit (CPU) coupled to the working memory and the machine readable data for performing a Fourier transformation of the machine readable data and for processing such data into crystal coordinates of three-dimensional molecule or complex of the peptide, and

[0033] (d) displaying a display coupled to the CPU for displaying the crystal coordinates of the three-dimensional moleculer or complex.

[0034] Other aspects, features, and advantages of the invention will be become apparent upon consideration of the detailed description below in conjunction with the appended figures.

BRIEF DESCRIPTION OF THE DRAWINGS

[0035] The file of this patent contains at least one drawing executed in color. Copies of this patent with color drawing(s) will be provided by the Patent and Trademark Office upon request and payment of the necessary fee.

[0036]FIGS. 1A and 1B depict the three-dimensional structure of the ERAB or HADH2 monomer. FIG. 1A shows the stereo Cα trace of the ERAB or HADH2 monomer. Every tenth residue is numbered. The bound NAD-inhibitor adduct is also shown. FIG. 1B is a ribbon diagram of the ERAB or HADH2 monomer, with the NAD-inhibitor adduct shown in ball-and-stick representation. The ribbon is white at the amino terminus and becomes darker blue moving toward the carboxy terminus. Alpha-carbon positions of residues in the insertion regions of ERAB or HADH2 are shown as yellow spheres.

[0037]FIG. 2 shows the sequence alignment of wild-type ERAB or HADH2 and representative members of the SDR family. The wild-type ERAB or HADH2 sequence is aligned with five related members of the SDR family: E. coli 7α-hydroxysteroid dehydrogenase (7α-HSD), Streptomyces hydrogenans 3α-20β-hydroxysteroid dehydrogenase (3α-20β-HSD), human 17β-hydrodroxysteroid dehydrogenase (17β-HSD), human 15-hydroxyprostaglandin dehydrogenase (15-PGD; P15428) (Ensor et al., Journal of Biochemistry, Vol. 265, pp. 14888-91 (1990)) and a human protein of unknown function, GenBank accession number CAA20237.1. 7α-HSD (1fmc) and 3α-20β-HSD (1hdc) are two proteins with known structures that are closely related to ERAB or HADH2; 17β-HSD (1fdt) is a similar human protein of known structure. A gapped sequence alignment for comparison is derived using Gapped BLAST [Altschul et al., Nucleic Acids Research, Vol. 25, pp. 3389-3402 (1997)] to search NCBI's GenBank database. Results indicate that 15-PGD is a human protein sequence similar to ERAB or HADH2; CAA20237.1 is a human nucleotide sequence that is similar when translated to its corresponding protein sequence. The alignment of ERAB or HADH2 to 17β-HSD, 7α-HSD, and 3α-20β-HSD was derived from a structural superposition using the tools in Insight II [available through Molecular Simulations Inc. (1999)] coupled with visual inspection. The sequences of 15-PGD and translated CAA20237.1 were aligned to the resulting profile using CLUSTALW [Thompson et al., Nucleic Acids Research, Vol. 22, pp. 4673-4680 (1994)]. Every tenth residue in ERAB or HADH2 is labeled. The secondary structure elements of ERAB or HADH2, as identified by PROCHECK (Laskowski et al., Journal of Applied Crystallography, Vol. 26, pp. 283-291 (1993)), are underlined and labeled above the sequences. Residues that are identical () or similar (∘) in all six proteins are marked beneath the sequences. The first six residues of ERAB or HADH2, which are disordered in the crystal structure, are not shown. The final 53 residues of 17β-HSD are also not shown.

[0038]FIG. 3 is a ribbon representation of the ERAB or HADH2 tetramer. The tetramer is viewed down one of three mutually perpendicular two-fold axes. Individual monomers are shown in red, green, blue and yellow. The bound NAD⁺ and NAD-inhibitor adduct molecules are shown in ball-and-stick representation.

[0039]FIG. 4A shows the structural formula and binding enantiomer of Compound I. FIG. 4B is a stereoview of the electron density for the NAD-Compound I adduct. FIG. 4C depicts the proposed reaction scheme occurring between the NAD⁺ and Compound I. FIG. 4D is a schematic LIGPLOT (Wallace et al., Protein England Vol. 8, pp. 127 -134 (1995)) view of ERAB or HADH2-Compound I interactions. Compound I, the C4N atom (see Table III) of NAD⁺, and the enzyme side-chains that form hydrogen bonds to the ligand are shown in ball-and-stick representation.

[0040]FIG. 5 is a plot of integrated-binding data obtained for a calorimetric titration of wild-type ERAB or HADH2 into Compound I in the presence and absence of cofactor. Wild-type ERAB or HADH2 (415 μM) was titrated into 20 μM inhibitor in the presence and absence of 20 μM cofactor at 15° C. The closed symbols represent the integrated-data points for 10 μL injections of ERAB or HADH2 into inhibitor in the absence of cofactor (♦); in the presence of NAD⁺ (); and in the presence of NADH (▪). The open symbols represent the integrated data points for the corresponding control titrations of ERAB or HADH2 into buffer (Δ); in the presence of NAD⁺ (∘); and in the presence of NADH (□). Lines connecting the data points have been added for visual clarity.

SEQUENCE LISTINGS

[0041] SEQ ID NO. 1—Full-length mutant ERAB or HADH2 C214R (nucleotide sequence—786 base pairs)

[0042] SEQ ID NO. 2—Full-length mutant ERAB or HADH2 C214R (peptide sequence—261 AA)

[0043] SEQ ID NO. 3—Full-length mutant ERAB or HADH2 C5V (nucleotide sequence—786 base pairs)

[0044] SEQ ID NO. 4—Full-length mutant ERAB or HADH2 C5V (peptide sequence—261 AA)

[0045] SEQ ID NO. 5—Full-length mutant ERAB or HADH2 C58V (nucleotide sequence—786 base pairs)

[0046] SEQ ID NO. 6—Full-length mutant ERAB or HADH2 C58V (peptide sequence—261 AA)

[0047] SEQ ID NO. 7—DNA sequence of wild-type ERAB or HADH2 (nucleotide sequence—786 base pairs)

[0048] SEQ ID NO. 8—Peptide sequence of wild-type ERAB or HADH2 (peptide sequence—261 AA)

[0049] SEQ ID NO. 9—PCR primer

[0050] SEQ ID NO. 10—PCR primer

[0051] SEQ ID NO. 11—Oligonucleotide for C5V

[0052] SEQ ID NO. 12—Oligonucleotide for C58V

[0053] SEQ ID NO. 13—Oligonucleotide for C214R

[0054] SEQ ID NO. 14—Peptide sequence of 7α-HDS

[0055] SEQ ID NO. 15—Peptide sequence of 3α20β-HDS

[0056] SEQ ID NO. 16—Peptide sequence of 17β-HDS

[0057] SEQ ID NO. 17—Peptide sequence of CAA20237.1

[0058] SEQ ID NO. 18—Peptide sequence of 15- PGD

[0059] SEQ ID NO. 19—Full-length mutant ERAB or HADH2 C214A (nucleotide sequence—786 base pairs)

[0060] SEQ ID NO. 20—Full-length mutant ERAB or HADH2 C214A (peptide sequence—261 AA)

[0061] SEQ ID NO. 21—Oligonucleotide for ERAB or HADH2 C214A

[0062] SEQ ID NO. 22—Full-length mutant ERAB or HADH2 C214S (nucleotide sequence—786 base pairs)

[0063] SEQ ID NO. 23—Full-length mutant ERAB or HADH2 C214S (peptide sequence—261 AA)

[0064] SEQ ID NO. 24—Oligonucleotide for ERAB or HADH2 C214S

DETAILED DESCRIPTION OF THE INVENTION

[0065] ERAB or HADH2 is a member of the short-chain dehydrogenase/reductase (SDR) family of enzymes. We have facilitated overexpression of several mutants of the enzyme in E. coli. The mutants having advantageous physical characteristics as compared to the wild-type ERAB or HADH2. The mutant ERAB or HADH2 peptides of the present invention have sufficient activity, stability and solubility so as to allow for peptide crystallization and subsequent x-ray crystallography characterization. Such properties facilitate the resolution of the three-dimensional crystal structure of human ERAB or HADH2 as well as the characterization of several structural features of ERAB or HADH2 responsible for interactions associated with high-affinity binding of substrates to ERAB or HADH2. Such interactions include the formation of a covalent linkage between the bound substrate and the NAD⁺ cofactor.

[0066] We have determined the crystal structure of human ERAB or HADH2 with NAD⁺ and an inhibitory small molecule bound thereto. The inhibitor occupies the substrate-binding site and forms a covalent adduct with the NAD⁺ cofactor. The crystal structure provides a basis for the design of ERAB or HADH2 inhibitors with potential application in the treatment of Alzheimer's disease. Crystals of ERAB or HADH2 with bound NAD⁺ and Compound I were obtained using the C214R mutant of the enzyme. This mutant was produced to avoid potential problems with cysteine oxidation in the protein, with arginine selected as the replacement amino acid because of its occurrence at this position in other mammalian ERAB or HADH2 sequences [He et al. (1998), supra]. Enzymatic activity of the C214R mutant protein is comparable to that of the wild-type protein. The crystal structure of the ERAB or HADH2:NAD⁺:Compound I complex was determined at 2.0 Å using molecular replacement techniques. The search model for molecular replacement was our 1.9 Å resolution structure of the mutant ERAB or HADH2:NAD⁺ complex. The structure was refined to an R factor of 0.215 for all data to 2.0 Å resolution. Data collection, structure determination, and refinement statistics are summarized in Table I. The resolution of the ERAB or HADH2 crystal structure allows for efficient design and development of inhibitors or modulators of human ERAB or HADH2. Inhibition of ERAB or HADH2 finds therapeutic utility in the treatment of AD. In addition to any therapeutic application, ERAB or HADH2 inhibitors can facilitate the delineation of the role of the enzyme in both normal cellular function and in Aβ pathogenesis.

[0067] The invention encompasses both the mutant peptides per se and salts thereof. The peptide may be synthetically or naturally produced. The invention further relates to an isolated, purified polynucleotide which encodes an enzymatically active peptide mutant of ERAB or HADH2 in the active conformation. The polynucleotide may be natural or recombinant.

[0068] The invention provides an expression vector for producing an enzymatically active mutant of human ERAB or HADH2 peptide in a host cell. The invention further relates to a host cell stably transformed and transfected with a polynucleotide encoding an enzymatically active peptide mutant of ERAB or HADH2, or fragment thereof, or an active functional analog thereof, in a manner allowing the expression of the enzymatically active peptide mutant of ERAB or HADH2 in the active conformation.

[0069] According to the present invention, an inhibitor (Compound I) of ERAB or HADH2 and the crystal structure of the ERAB or HADH2:NAD⁺:inhibitor complex are provided. The availability of a potent specific inhibitor of ERAB or HADH2 can facilitate the detailed analysis of the role of this enzyme in AD pathogenesis and may ultimately provide a new therapeutic approach for treatment of the disease. The crystal structure of the enzyme:inhibitor:cofactor complex provides a basis for the design of additional inhibitors and for elucidating the nature of the interactions between ERAB or HADH2 and the amyloid-β peptide.

[0070] The molecular structure of the x-ray crystallography data may be used to model the binding of candidate compounds in order to screen candidate compounds. In accordance with the invention, there is also provided several structural features unique to ERAB or HADH2 as compared to other members of the short-chain dehydrogenase/reductase (SDR) family. Some of these features are responsible for the high-affinity binding of an inhibitor compound to the ERAB or HADH2 substrate-binding site, including the formation of a covalent linkage between inhibitor and the NAD⁺ cofactor.

[0071] Potential inhibitors or modulators of the human ERAB or HADH2 may be identified according to the method of the present invention. Potential therapeutic compounds for the treatment of various disease conditions associated with the ERAB or HADH2, for example neurodegenerative diseases and cancers may be designed and screened according to the present invention. In the designing and screening processes, the DNA sequence or variants thereof encoding the mutant ERAB or HADH2 peptide is expressed, and may be assayed for interaction of the enzyme with the candidate compound by exposing the enzyme to the candidate compound and evaluating the interaction of the enzyme with the candidate compound. The designing and synthesis as well as screening may be automated, for example, utilizing robotic techniques.

[0072] Three-dimensional molecular structure of ERAB or HADH2 of the present invention may be used to model the binding of candidate compounds to the ERAB or HADH2 binding site, facilitating screening candidate compounds. The x-ray crystallographic coordinates disclosed herein, allow for the generation of three-dimensional models of the catalytic region and binding site of the human ERAB or HADH2. Design of inhibitors generally involves the generation of molecules via the use of computer programs, which build and link fragments or atoms into a site based upon steric and electrostatic complementary, without reference to substrate analog structures. The drug design process begins after the structure of the target (human ERAB or HADH2) is solved to at least a resolution of 3 Å, more preferably 2.5 Å, even more preferably 2 Å. Refinement of the structure to a resolution of 2 Å or better with fixed water molecules in place provides more optimal conditions to undertake drug design.

[0073] In one preferred embodiment, the method of screening utilized the steps of (a) computer-generating a virtual-binding cavity, the binding cavity defined by the binding sites; (b) computer-generating a compound structure that spatially conforms to the binding cavity; and (c) testing to see whether said compound binds to at least one of the stated-binding sites.

[0074] The invention also has utility in the iterative drug design process. The process screens potential inhibitors or modulators of the ERAB or HADH2 enzyme by determining their ability to bind to and inhibit or modulate the ERAB or HADH2. The x-ray crystallographic coordinates disclosed herein allow advantageously generation of three-dimensional models of the enzymatically active site and the drug-binding site of the ERAB or HADH2 protein. De novo design comprises of the generation of molecules via the use of computer programs which build and link fragments or atoms into a site based upon steric and electrostatic complementarily, without reference to substrate analog structures. The determination of the structure of the target (human ERAB or HADH2) is solved to at least a resolution of 3 Å, more preferably 2.5 Å, even more preferably 2 Å. Refinement of the structure to a resolution of 2 Å or better with fixed water molecules in place provides more optimal conditions to undertake drug design.

[0075] In one preferred embodiment, the method for identifying potential inhibitors utilizes the steps of (a) designing a potential inhibitor or modulator for ERAB or HADH2 that will interact with amino acids in the ERAB or HADH2 substrate-binding site based on the crystal coordinates of the mutant ERAB or HADH2 peptide:ligand:NAD⁺ complex set forth in Table II; and (b) synthesizing the potential inhibitor or modulator and assaying it to determine whether it inhibits or modulates the activity of ERAB or HADH2.

[0076] Rapidly screening methods to assay those compounds that inhibit or modulate the ERAB or HADH2 enzyme or core structure for further ERAB or HADH2 inhibitor design may be used. The high throughput-screening assay is capable of being fully automated on robotic workstations. The assay may employ radioactivity or other materials useful for detection.

[0077] A computer processor may be used for analyzing a molecular structure comprising by using a machine-readable data storage medium comprising a data storage material encoded with machine-readable data. The data comprises crystal coordinates of mutant ERAB or HADH2 peptide molecule or its molecular complex. In this method, a CPU coupled to a working memory and the machine readable data may be used to perform a Fourier transformation of the machine readable data and to process such data into crystal coordinates of three-dimensional molecule or complex of said peptide. The x-ray coordinate data may be processed into three-dimensional graphical display using a computer-based method. The machine-readable data storage medium may include CD-ROM, magneto-optic disk, or other storage media.

[0078] The terms as used herein are explained below. Also, as used herein, the terms “comprising” and “including” are used in the conventional, non-limiting sense.

[0079] A. Peptides, Proteins and Antibodies

[0080] The present invention provides isolated peptide and protein molecules that consist of, consist essentially of or are comprised of the amino acid sequences of the mutant peptides encoded by the nucleic acid sequences disclosed in the SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19 and SEQ ID NO: 22 as well as all obvious variants of these peptides that the within the art to make and use. Some of these variants are described in detail below.

[0081] The invention also includes a modified, enzymatically active ERAB or HADH2 peptide comprising a fold, wherein said fold comprises: a core β-sheet of seven strands sandwiched between two sets of three α-helices; and first and second insert domains, relative to other members of the SDR family, the first insert domain forming a β hairpin that extends the surface of said ERAB or HADH2 peptide on one side of a substrate-binding cleft, and the second insert domain extending a loop between an α-helix comprising residues 123-136 and a β-sheet comprising residues 148-153 of SEQ ID NO: 2. The invention provides a peptide having an amino acid sequence comprising amino acids 90 to 261 of SEQ ID NO. 2 or an active or functional variant thereof.

[0082] As used herein, a peptide is said to be “isolated” or “purified” when it is substantially free of homologous cellular material or free of chemical precursors or other chemicals. The peptides of the present invention can be purified to homogeneity or other degrees of purity. The level of purification will be based on the intended use. The critical feature is that the preparation allows for the desired function of the peptide, even if in the presence of considerable amounts of other components.

[0083] In some uses, “substantially free of cellular material” includes preparations of the peptide having less than 30% (by dry weight) other proteins (i.e., contaminating protein), preferably less than 20% other proteins, more preferably less than 10% other proteins, or most preferably less than 5% other proteins. When the peptide is recombinantly produced, it can also be substantially free of culture medium, i.e., culture medium represents less than 20% of the volume of the protein preparation.

[0084] The language “substantially free of chemical precursors or other chemicals” includes preparations of the peptide in which it is separated from chemical precursors or other chemicals that are involved in its synthesis. In one embodiment, the language “substantially free of chemical precursors or other chemicals” includes preparations of the mutant peptide having less than 30% (by dry weight) chemical precursors or other chemicals, preferably less than 20% chemical precursors or other chemicals, more preferably less than 10% chemical precursors or other chemicals, or most preferably less than 5% chemical precursors or other chemicals.

[0085] The isolated mutant peptide described herein can be purified from cells that naturally express it, purified from cells that have been altered to express it (recombination), or synthesized using known protein synthesis methods. For example, a nucleic acid molecule encoding the mutant peptide is cloned into an expression vector, the expression vector introduced into a host cell and the peptide expressed in the host cell. The peptide can then be isolated from the cells by an appropriate purification scheme using standard peptide/protein purification techniques. Many of these techniques are described in detail below.

[0086] As mentioned above, the present invention also provides and enables obvious variants of the amino acid sequence of the peptides of the present invention, such as naturally occurring mature forms of the peptides, allelic/sequence variants of the peptides, non-naturally occurring recombinantly derived variants of the peptides, and orthologs and paralogs of the peptides. Such variants can be generated using techniques that are known by those skilled in the fields of recombinant nucleic acid technology and protein biochemistry.

[0087] Such variants can readily be identified/made using molecular techniques and the sequence information disclosed herein. Further, such variants can readily be distinguished from other peptides based on sequence and/or structural homology to the peptides of the present invention. The degree of homology/identity present will be based primarily on whether the peptide is a functional variant or non-functional variant, the amount of divergence present in the paralog family and the evolutionary distance between the orthologs.

[0088] To determine the percent identity of two amino acid sequences or two nucleic acid sequences, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in one or both of a first and a second amino acid or nucleic acid sequence for optimal alignment and non-homologous sequences can be disregarded for comparison purposes). The length of a reference sequence aligned for comparison purposes is at least 30%, preferably 40%, more preferably 50%, even more preferably 60% or more of the length of the reference sequence. In a preferred embodiement, the length of a reference sequence aligned for comparison purposes is at least 70%, preferably 80%, more preferably 90% or more of the length of the reference sequence. The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position (as used herein amino acid or nucleic acid ‘identity’ is equivalent to amino acid or nucleic acid ‘homology’). The percent identity between the two sequences is a function of the number of identical positions shared by the sequences, taking into account the number of gaps, and the length of each gap, which need to be introduced for optimal alignment of the two sequences.

[0089] The comparison of sequences and determination of percent identity and similarity between two sequences can be accomplished using a mathematical algorithm. (See, e.g., Computational Molecular Biology, Lesk, A. M., ed., Oxford University Press, New York, 1988; Biocomputing: Informatics and Genome Projects, Smith, D. W., ed., Academic Press, New York, 1993; Computer Analysis of Sequence Data, Part 1, Griffin, A. M., and Griffin, H. G., eds., Humana Press, New Jersey, 1994; Sequence Analysis in Molecular Biology, von Heinje, G., Academic Press, 1987; and Sequence Analysis Primer, Gribskov, M. and Devereux, J., eds., M Stockton Press, New York, 1991). In a preferred embodiment, the percent identity between two amino acid sequences is determined using the Needleman and Wunsch (J. Mol. Biol (48):444-453 (1970)) algorithm which has been incorporated into commercially available computer programs, such as GAP in the GCG software package, using either a Blossom 62 matrix or a PAM250 matrix, and a gap weight of 16, 14, 12, 10, 8, 6, or 4 and a length weight of 1, 2, 3, 4, 5, or 6. In yet another preferred embodiment, the percent identity between two nucleotide sequences can be determined using the commercially available computer programs including the GAP program in the GCG software package (Devereux, J., et al., Nucleic Acids Res. 12(1):387 (1984)), the NWS gap DNA CMP matrix and a gap weight of 40, 50, 60, 70, or 80 and a length weight of 1, 2, 3, 4, 5, or 6. In another embodiment, the percent identity between two amino acid or nucleotide sequences is determined using the algorithm of E. Meyers and W. Miller (CABIOS, 4:11-17 (1989)) which has been incorporated into commercially available computer programs, such as ALIGN (version 2.0), using a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4.

[0090] The nucleic acid and protein sequences of the present invention can further be used as a “query sequence” to perform a search against sequence databases to, for example, identify other family members or related sequences. Such searches can be performed using commercially available search engines, such as the NBLAST and XBLAST programs (version 2.0) of Altschul, et al. (J. Mol. Biol. 215:403-10 (1990)). BLAST nucleotide searches can be performed with the NBLAST program, score=100, wordlength=12 to obtain nucleotide sequences homologous to the nucleic acid molecules of the invention. BLAST protein searches can be performed with the XBLAST program, score=50, wordlength=3 to obtain amino acid sequences homologous to the proteins of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al. (Nucleic Acids Res. 25(17):3389-3402 (1997)). When utilizing BLAST programs, the default parameters of the respective programs (e.g., XBLAST and NBLAST) can be used.

[0091] Full-length clones comprising one of the peptides of the present invention can readily be identified as having complete sequence identity to one of the mutant peptides of human ERAB or HADH2 of the present invention as well as being encoded by the same genetic locus as the mutant peptide provided herein.

[0092] Allelic variants of a peptide can readily be identified as having a high degree (significant) of sequence homology/identity to at least a portion of the peptide as well as being encoded by the same genetic locus as the mutant peptide provided herein. As used herein, two proteins (or a region of the proteins) have significant homology when the amino acid sequences are typically at least 70%, preferably 75%, more preferably 80% or 85%, and typically at least 90%, more preferably 95% or more homologous. A significantly homologous amino acid sequence, according to the present invention, will be encoded by a nucleic acid sequence that will hybridize to a peptide encoding nucleic acid molecule under stringent conditions as described below.

[0093] Paralogs of a peptide can readily be identified as having some degree of significant sequence homology/identity to at least a portion of the mutant peptide as well as being encoded by a gene from human, and as having similar activity or function. Two proteins will typically be considered paralogs when the amino acid sequences are typically at least 70%, preferably 80%, more preferably at least 90%, most preferably 95% or more homologous through a given region or domain. Such paralogs will be encoded by a nucleic acid sequence that will hybridize to a mutant peptide encoding nucleic acid molecule under stringent conditions as described in the section “B. Nucleic Acids and Polynucleotides” below.

[0094] Orthologs of a mutant peptide can readily be identified as having some degree of significant sequence homology/identity to at least a portion of the mutant peptide as well as being encoded by a gene from another organism. Preferred orthologs will be isolated from mammals other than human, for the development of human therapeutic targets and agents, or other invertebrates, particularly insects of economical/agriculture importance, e.g. members of the Lepidopteran and Coleopteran orders, for the development of insecticides and insecticidal targets. Such orthologs will be encoded by a nucleic acid sequence that will hybridize to a mutant peptide encoding nucleic acid molecule under moderate to highly stringent conditions, as more fully described below, depending on the degree of relatedness of the two organisms yielding the proteins.

[0095] Non-naturally occurring variants of the mutant peptides of the present invention can readily be generated using recombinant techniques. Such variants include, but are not limited to deletions, additions and substitutions in the amino acid sequence of the mutant peptide. For example, one class of substitutions involves conserved amino acid changes. Such substitutions are those that substitute a given amino acid in a peptide by another amino acid of like characteristics. Typically seen as conservative substitutions are the replacements, one for another, among the aliphatic amino acids Ala, Val, Leu, and Ile; interchange of the hydroxyl residues Ser and Thr; exchange of the acidic residues Asp and Glu; substitution between the amide residues Asn and Gln; exchange of the basic residues Lys and Arg; and replacements among the aromatic residues Phe, Tyr. Guidance concerning which amino acid changes are likely to be phenotypically silent are found in Bowie et al., Science 247:1306-1310 (1990).

[0096] Variants of the mutant peptide can be fully functional or can lack function in one or more activities. Fully functional variants typically contain only conservative variation or variation in non-critical residues or in non-critical regions. Functional variants can also contain substitution of similar amino acids, which result in no change or an insignificant change in function. Alternatively, such substitutions may positively or negatively affect function to some degree.

[0097] Non-functional variants typically contain one or more non-conservative amino acid substitutions, deletions, insertions, inversions, or truncation or a substitution, insertion, inversion, or deletion in a critical residue or critical region.

[0098] Amino acids that are essential for function can be identified by methods known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham et al., Science 244:1081-1085 (1989)). The latter procedure introduces single alanine mutations at every residue in the molecule. The resulting mutant molecules are then tested for biological activity such as receptor binding or in vitro proliferative activity. Sites that are critical for binding can also be determined by structural analysis such as x-ray crystallography, nuclear magnetic resonance or photoaffinity labeling (Smith et al., J. Mol. Biol. 224:899-904 (1992); de Vos et al. Science 255:306-312 (1992)). Accordingly, the polypeptides also encompass derivatives or analogs in which a substituted amino acid residue is not one encoded by the genetic code; in which a substituent group is included, in which the mature polypeptide is fused with another compound, such as a compound to increase the half-life of the polypeptide (for example, polyethylene glycol), or in which the additional amino acids are fused to the mature polypeptide, such as a leader or secretory sequence or a sequence for purification of the mature polypeptide or a pro-protein sequence.

[0099] “Polypeptide” refers to any peptide or protein comprising two or more amino acids joined to each other by peptide bonds or modified peptide bonds, i.e., peptide isosteres. “Polypeptide” refers to both short chains, commonly referred to as peptides, oligopeptides or oligomers, and to longer chains, generally referred to as proteins. The terms “peptide”, “polypeptide” and “protein” are used interchangeably herein. Polypeptides may contain amino acids other than the 20 naturally occurring amino acids. Further, many amino acids, including the terminal amino acids, may be modified by natural processes, such as processing and other post-translational modifications, or by chemical modification techniques well known in the art. Common modifications that occur naturally in polypeptides are described in basic texts, detailed monographs, and the research literature, and they are well known to those of skill in the art. Generally known modifications include, but are not limited to, acetylation, acylation, ADP-ribosylation, amidation, covalent attachment of flavin, covalent attachment of a heme moiety, covalent attachment of a nucleotide or nucleotide derivative, covalent attachment of a lipid or lipid derivative, covalent attachment of phosphotidylinositol, cross-linking, cyclization, disulfide bond formation, demethylation, formation of covalent crosslinks, formation of cystine, formation of pyroglutamate, formylation, gamma carboxylation, glycosylation, GPI anchor formation, hydroxylation, iodination, methylation, myristoylation, oxidation, proteolytic processing, phosphorylation, phenylation, racemization, selenoylation, sulfation, transfer-RNA mediated addition of amino acids to proteins such as arginylation, and ubiquitination. Several particularly common modifications, glycosylation, lipid attachment, sulfation, gamma-carboxylation of glutamic acid residues, hydroxylation and ADP-ribosylation, for instance, are described in most basic texts, such as Creighton, Proteins—Structure and Molecular Properties, 2nd Ed., W. H. Freeman and Company, New York (1993). Many reviews are available on this subject, such as Wold, Posttranslational Covalent Modification of Proteins, B. C. Johnson, Ed., Academic Press, New York 1-12 (1983); Seifter et al. (Meth. Enzymol. 182:626-646 (1990)) and Rattan et al. (Ann. N.Y. Acad. Sci. 663:48-62 (1992)).

[0100] The present invention further provides for fragments of the mutant peptides, in addition to proteins and peptides that comprises and consist of such fragments.

[0101] As used herein, a fragment comprises at least 8 or more contiguous amino acid residues from the mutant peptide of ERAB or HADH2. Such fragments can be chosen based on the ability to retain one or more of the biological activities of the ERAB or HADH2 or could be chosen for the ability to perform a function, e.g. act as an immunogen. Particularly important fragments are biologically active fragments, peptides which are, for example about 8 or more amino acids in length. Such fragments will typically comprise a domain or motif of the mutant peptide, e.g., active site. Further, possible fragments include, but are not limited to, domain or motif containing fragments, soluble peptide fragments, and fragments containing immunogenic structures. Predicted domains and functional sites are readily identifiable by computer programs well-known and readily available to those of skill in the art (e.g., by PROSITE analysis).

[0102] The peptides of the present invention can be attached to heterologous sequences to form chimeric or fusion proteins. Such chimeric and fusion proteins comprise a peptide operatively linked to a heterologous protein having an amino acid sequence not substantially homologous to the mutant peptide of ERAB or HADH2. “Operatively linked” indicates that the peptide and the heterologous protein are fused in-frame. The heterologous protein can be fused to the N-terminus or C-terminus of the mutant peptide of ERAB or HADH2. The two peptides linked in a fusion peptide are typically derived from two independent sources, and therefore a fusion peptide comprises two linked peptides not normally found linked in nature. The two peptides may be from the same or different genome.

[0103] In some uses, the fusion protein does not affect the activity of the peptide per se. For example, the fusion protein can include, but is not limited to, enzymatic fusion proteins, for example beta-galactosidase fusions, yeast two-hybrid GAL fusions, poly-His fusions, MYC-tagged, HI-tagged and Ig fusions. Such fusion proteins, particularly poly-His fusions, can facilitate the purification of recombinant peptide. In certain host cells (e.g., mammalian host cells), expression and/or secretion of a protein can be increased by using a heterologous signal sequence.

[0104] A chimeric or fusion protein can be produced by standard recombinant DNA techniques. For example, DNA fragments coding for the different protein sequences are ligated together in-frame in accordance with conventional techniques. In another embodiment, the fusion gene can be synthesized by conventional techniques including automated DNA synthesizers. Alternatively, PCR amplification of gene fragments can be carried out using anchor primers which give rise to complementary overhangs between two consecutive gene fragments which can subsequently be annealed and re-amplified to generate a chimeric gene sequence [see Ausubel et al., Current Protocols in Molecular Biology (1992)]. Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST protein). A mutant ERAB or HADH2 peptide-encoding nucleic acid can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the mutant peptide.

[0105] B. Nucleic Acids and Polynucleotides

[0106] The present invention provides isolated nucleic acid molecules that encode the functional, active mutant peptides of ERAB or HADH2 of the present invention. Such nucleic acid molecules will consist of, consist essentially of, or comprise a nucleotide sequence that encodes one of the peptides of the present invention, an allelic variant thereof, or an ortholog or paralog thereof.

[0107] As used herein, an “isolated” nucleic acid molecule is one that is separated from other nucleic acid present in the natural source of the nucleic acid. Preferably, an “isolated” nucleic acid is free of sequences which naturally flank the nucleic acid (i.e., sequences located at the 5′ and 3′ ends of the nucleic acid) in the genomic DNA or cDNA of the organism from which the nucleic acid is derived. However, there can be some flanking nucleotide sequences, for example up to about 5KB, particularly contiguous peptide encoding sequences and peptide encoding sequences within the same gene but separated by introns in the genomic sequence. The important point is that the nucleic acid is isolated from remote and unimportant flanking sequences such that it can be subjected to the specific manipulations described herein such as recombinant expression, preparation of probes and primers, and other uses specific to the nucleic acid sequences.

[0108] Moreover, an “isolated” nucleic acid molecule, such as a cDNA molecule, can be substantially free of other cellular material, or culture medium when produced by recombinant techniques, or chemical precursors or other chemicals when chemically synthesized. However, the nucleic acid molecule can be fused to other coding or regulatory sequences and still be considered isolated.

[0109] For example, recombinant DNA molecules contained in a vector are considered isolated. Further examples of isolated DNA molecules include recombinant DNA molecules maintained in heterologous host cells or purified (partially or substantially) DNA molecules in solution. Isolated RNA molecules include in vivo or in vitro RNA transcripts of the isolated DNA molecules of the present invention. Isolated nucleic acid molecules according to the present invention further include such molecules produced synthetically.

[0110] Full-length genes may be cloned from known sequence using any one of a number of methods known in the art. For example, a method which employs XL-PCR (Perkin-Elmer, Foster City, Calif.) to amplify long pieces of DNA may be used. Other methods for obtaining full-length sequences are known in the art.

[0111] The isolated nucleic acid molecules can encode the active protein plus additional amino or carboxyl-terminal amino acids, or amino acids interior to the mature peptide (when the mature form has more than one peptide chain, for instance). Such sequences may play a role in processing of a protein from precursor to an active form, facilitate protein trafficking, prolong or shorten protein half-life or facilitate manipulation of a protein for assay or production, among other things. As generally is the case in situ, the additional amino acids may be processed away from the mature protein by cellular enzymes. As mentioned above, the isolated nucleic acid molecules include, but are not limited to, the sequence encoding the active mutant peptide of ERAB or HADH2 alone or in combination with coding sequences, such as a leader or secretory sequence (e.g., a pre-pro or pro-protein sequence), the sequence encoding the active mutant peptide, with or without the additional coding sequences, plus additional non-coding sequences, for example introns and non-coding 5′ and 3′ sequences such as transcribed but non-translated sequences that play a role in transcription, including mRNA processing (including splicing and polyadenylation signals), ribosome binding sites and sequences important for stability of MRNA. In addition, the nucleic acid molecule may be fused to a marker sequence encoding, for example, a peptide that facilitates purification.

[0112] Isolated nucleic acid molecules can be in the form of RNA, such as mRNA, or in the form of DNA, including cDNA and genomic DNA, obtained by cloning or produced by chemical synthetic techniques or by a combination thereof. The nucleic acid, especially DNA, can be double-stranded or single-stranded. Single-stranded nucleic acid can be the coding strand (sense strand) or the non-coding strand (antisense strand).

[0113] The invention further provides nucleic acid molecules that encode fragments of the peptides of the present invention and that encode obvious variants of the peptides of the present invention that are described herein. Such nucleic acid molecules may be naturally occurring, such as allelic variants (same locus), paralogs (different locus), and orthologs (different organism), or may be constructed by recombinant DNA methods or by chemical synthesis. Such non-naturally occurring variants may be made by mutagenesis techniques, including those applied to nucleic acid molecules, cells, or organisms. Accordingly, as discussed above, the variants can contain nucleotide substitutions, deletions, inversions and insertions. Variation can occur in either or both the coding and non-coding regions. The variations can produce both conservative and non-conservative amino acid substitutions.

[0114] A fragment comprises a contiguous nucleotide sequence greater than 12 or more nucleotides. Further, a fragment could be at least 30, preferably 40, more preferably 50, even more preferably 100, most preferably 250 or 500 nucleotides in length. The length of the fragment will be based on its intended use. For example, the fragment can encode epitope bearing regions of the peptide, or can be useful as DNA probes and primers. Such fragments can be isolated using the known nucleotide sequence to synthesize an oligonucleotide probe. A labeled probe can then be used to screen a cDNA library, genomic DNA library, or MRNA to isolate nucleic acid corresponding to the coding region. Further, primers can be used in PCR reactions to clone specific regions of gene.

[0115] A probe/primer typically comprises a substantially purified oligonucleotide or oligonucleotide pair. The oligonucleotide typically comprises a region of nucleotide sequence that hybridizes under stringent conditions to at least 12, preferably 20, more preferably 25, even more preferably 40, most preferably 50 or more consecutive nucleotides.

[0116] Orthologs, homologs, and allelic variants can be identified using methods known in the art. As described above, these variants comprise a nucleotide sequence encoding a peptide that is typically 60%, preferably 70%, more preferably 80%, even more preferably 85%, and typically at least 90%, preferably 95% or more homologous to the nucleotide sequence provided in SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19 or SEQ ID NO: 22, or a fragment of these sequences. Such nucleic acid molecules can readily be identified as being able to hybridize under moderate to highly stringent conditions, to the nucleotide sequences shown in SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19 or SEQ ID NO: 22, or a fragment thereof.

[0117] As used herein, the term “hybridizes under stringent conditions” is intended to describe conditions for hybridization and washing under which nucleotide sequences encoding a peptide at least 50%, preferably 55% or more homologous to each other typically remain hybridized to each other. The conditions can be such that sequences at least 65%, preferably 70%, more preferably 75% or more homologous to each other typically remain hybridized to each other. Standard hybridization conditions from moderate to highly stringent conditions are known to those skilled in the art (See e.g., Current Protocols in Molecular Biology, John Wiley & Sons, N.Y. (1989), 6.3.1-6.3.6). Moderate hybridization conditions are defined as equivalent to hybridization in 2×sodium chloride/sodium citrate (SSC) at 30° C., followed by one or more washes in 1×SSC, 0.1% SDS at 50-60° C. Highly stringent conditions are defined as equivalent to hybridization in 6×sodium chloride/sodium citrate (SSC) at 45° C., followed by one or more washes in 0.2×SSC, 0.1% SDS at 50-65° C.

[0118] The nucleic acid molecules of the present invention are useful for probes, primers, chemical intermediates, and in biological assays. The nucleic acid molecules are useful as a hybridization probe for cDNA and genomic DNA to isolate full-length cDNA and genomic clones encoding the peptide described herein and to isolate cDNA and genomic clones that correspond to variants (alleles, orthologs, etc.) producing the same or related peptides described herein.

[0119] The probe can correspond to any sequence along the entire length of the nucleic acid molecules provided in the SEQ ID NO: 1, SEQ ID NO: 3. SEQ ID NO: 5, SEQ ID NO: 19 or SEQ ID NO: 22. Accordingly, it could be derived from 5′ noncoding regions, the coding region, and 3′ noncoding regions.

[0120] The nucleic acid molecules are also useful as primers for PCR to amplify any given region of a nucleic acid molecule and are useful to synthesize antisense molecules of desired length and sequence.

[0121] The nucleic acid molecules are also useful for constructing recombinant vectors. Such vectors include expression vectors that express a portion of, or all of, the peptide sequences. Vectors also include insertion vectors, used to integrate into another nucleic acid molecule sequence, such as into the cellular genome, to alter in situ expression of a gene and/or gene product. For example, an endogenous coding sequence can be replaced via homologous recombination with all or part of the coding region containing one or more specifically introduced mutations.

[0122] The nucleic acid molecules are also useful for expressing antigenic portions of the proteins; for determining the chromosomal positions of the nucleic acid molecules by means of in situ hybridization methods; for designing ribozymes corresponding to all, or a part, of the mRNA produced from the nucleic acid molecules described herein; for constructing host cells expressing a part, or all, of the nucleic acid molecules and peptides; for constructing transgenic animals expressing all, or a part, of the nucleic acid molecules and peptides; and for making vectors that express part, or all, of the peptides.

[0123] The nucleic acid molecules are also useful as hybridization probes for determining the presence, level, form and distribution of nucleic acid expression. Accordingly, the probes can be used to detect the presence of, or to determine levels of, a specific nucleic acid molecule in cells, tissues, and in organisms. The nucleic acid whose level is determined can be DNA or RNA. Accordingly, probes corresponding to the peptides described herein can be used to assess expression and/or gene copy number in a given cell, tissue, or organism. These uses are relevant for diagnosis of disorders involving an increase or decrease in protein expression relative to normal results.

[0124] In vitro techniques for detection of mRNA include Northern hybridizations and in situ hybridizations. In vitro techniques for detecting DNA include Southern hybridizations and in situ hybridization.

[0125] Probes can be used as a part of a diagnostic test kit for identifying cells or tissues that express a protein.

[0126] C. Vectors and Host Cells

[0127] The invention also provides vectors containing the nucleic acid molecules described herein. The term “vector” refers to a vehicle, preferably a nucleic acid molecule, that can transport the nucleic acid molecules. When the vector is a nucleic acid molecule, the nucleic acid molecules are covalently linked to the vector nucleic acid. With this aspect of the invention, the vector includes a plasmid, single or double stranded phage, a single or double stranded RNA or DNA viral vector, or artificial chromosome, such as a BAC, PAC, YAC, OR MAC. Various expression vectors can be used to express polynucleotide encoding the mutant peptide of human ERAB or HADH2.

[0128] A vector can be maintained in the host cell as an extrachromosomal element where it replicates and produces additional copies of the nucleic acid molecules. Alternatively, the vector may integrate into the host cell genome and produce additional copies of the nucleic acid molecules when the host cell replicates.

[0129] The invention provides vectors for the maintenance (cloning vectors) or vectors for expression (expression vectors) of the nucleic acid molecules. The vectors can function in prokaryotic or eukaryotic cells or in both (shuttle vectors).

[0130] Expression vectors contain cis-acting regulatory regions that are operably linked in the vector to the nucleic acid molecules such that transcription of the nucleic acid molecules is allowed in a host cell. The nucleic acid molecules can be introduced into the host cell with a separate nucleic acid molecule capable of affecting transcription. Thus, the second nucleic acid molecule may provide a trans-acting factor interacting with the cis-regulatory control region to allow transcription of the nucleic acid molecules from the vector. Alternatively, a trans-acting factor may be supplied by the host cell. Finally, a trans-acting factor can be produced from the vector itself. It is understood, however, that in some embodiments, transcription and/or translation of the nucleic acid molecules can occur in a cell-free system.

[0131] The regulatory sequences to which the nucleic acid molecules described herein can be operably linked include promoters for directing mRNA transcription. These include, but are not limited to, the left promoter from bacteriophage λ, the lac, TRP, and TAC promoters from E. coli, the early and late promoters from SV40, the CMV immediate early promoter, the adenovirus early and late promoters, and retrovirus long-terminal repeats (LTR).

[0132] In addition to control regions that promote transcription, expression vectors may also include regions that modulate transcription, such as repressor binding sites and enhancers. Examples include the SV40 enhancer, the cytomegalovirus immediate early enhancer, polyoma enhancer, adenovirus enhancers, and retrovirus LTR enhancers.

[0133] In addition to containing sites for transcription initiation and control, expression vectors can also contain sequences necessary for transcription termination and, in the transcribed region a ribosome-binding site for translation. Other regulatory control elements for expression include initiation and termination codons as well as polyadenylation signals. The person of ordinary skill in the art would be aware of the numerous regulatory sequences that are useful in expression vectors. Such regulatory sequences are described, for example, in Sambrook et al., (Molecular Cloning: A Laboratory Manual. 2nd. ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., (1989)).

[0134] A variety of expression vectors can be used to express a nucleic acid molecule. Such vectors include chromosomal, episomal, and virus-derived vectors, for example vectors derived from bacterial plasmids, from bacteriophage, from yeast episomes, from yeast chromosomal elements, including yeast artificial chromosomes, from viruses such as baculoviruses, papovaviruses such as SV40, Vaccinia viruses, adenoviruses, poxviruses, pseudorabies viruses, and retroviruses. Vectors may also be derived from combinations of these sources such as those derived from plasmid and bacteriophage genetic elements, e.g., cosmids and phagemids. Appropriate cloning and expression vectors for prokaryotic and eukaryotic hosts are described in Sambrook et al., Molecular Cloning: A Laboratory Manual. 2nd. ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., (1989).

[0135] The regulatory sequence may provide constitutive expression in one or more host cells (i.e. tissue specific) or may provide for inducible expression in one or more cell types such as by temperature, nutrient additive, or exogenous factor such as a hormone or other ligand. A variety of vectors providing for constitutive and inducible expression in prokaryotic and eukaryotic hosts are known to those of ordinary skill in the art.

[0136] The nucleic acid molecules can be inserted into the vector nucleic acid by well-known methodology. Generally, the DNA sequence that will ultimately be expressed is joined to an expression vector by cleaving the DNA sequence and the expression vector with one or more restriction enzymes and then ligating the fragments together. Procedures for restriction enzyme digestion and ligation are known to those of ordinary skill in the art.

[0137] The vector containing the appropriate nucleic acid molecule can be introduced into an appropriate host cell for propagation or expression using well-known techniques. Bacterial cells include, but are not limited to, E. coli, Streptomyces, and Salmonella typhimurium. Eukaryotic cells include, but are not limited to, yeast, insect cells such as Drosophila, animal cells such as COS and CHO cells, and plant cells.

[0138] It may be desirable to express a peptide of the present invention as a fusion protein. Accordingly, the invention provides fusion vectors that allow for the production of such peptides. Fusion vectors can increase the expression of a recombinant protein, increase the solubility of the recombinant protein, and aid in the purification of the protein by acting for example as a ligand for affinity purification. A proteolytic cleavage site may be introduced at the junction of the fusion moiety so that the desired peptide can ultimately be separated from the fusion moiety. Proteolytic enzymes include, but are not limited to, factor Xa, thrombin, and enterokinase. Typical fusion expression vectors include pGEX (Smith et al., (1988) Gene 67:31-40), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) which fuse glutathione S-transferase (GST), maltose E binding protein, or protein A, respectively, to the target recombinant protein. Examples of suitable inducible non-fusion E. coli expression vectors include pTrc (Amann et al., (1988) Gene 69:301-315) and pET 11d (Studier et al., (1990) Gene Expression Technology: Methods in Enzymology 185:60-89).

[0139] Recombinant protein expression can be maximized in a host bacteria by providing a genetic background wherein the host cell has an impaired capacity to proteolytically cleave the recombinant protein. (Gottesman, S., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990) 119-128). Alternatively, the sequence of the nucleic acid molecule of interest can be altered to provide preferential codon usage for a specific host cell, for example E. coli. (Wada et al., (1992) Nucleic Acids Res. 20:2111-2118).

[0140] The nucleic acid molecules can also be expressed by expression vectors that are operative in yeast. Examples of vectors for expression in yeast e.g., S. cerevisiae include pYepSec1 (Baldari, et al., (1987) EMBO J. 6:229-234), pMFa (Kurjan et al., (1982) Cell 30:933-943), pJRY88 (Schultz et al., (1987) Gene 54:113-123), and pYES2 (Invitrogen Corporation, San Diego, Calif.).

[0141] The nucleic acid molecules can also be expressed in insect cells using, for example, baculovirus expression vectors. Baculovirus vectors available for expression of proteins in cultured insect cells (e.g., Sf 9 cells) include the pAc series (Smith et al., (1983) Mol. Cell Biol. 3:2156-2165) and the pVL series (Lucklow et al., (1989) Virology 170:31-39).

[0142] In certain embodiments of the invention, the nucleic acid molecules described herein are expressed in mammalian cells using mammalian expression vectors. Examples of mammalian expression vectors include pCDM8 (Seed, B. (1987) Nature 329:840) and pMT2PC (Kaufman et al., (1987) EMBO J. 6:187-195).

[0143] The expression vectors listed herein are provided by way of example only of the well-known vectors available to those of ordinary skill in the art that would be useful to express the nucleic acid molecules. Preferred vectors include the pET28a (Novagen, Madison, Wis.), pAcSG2 (Pharmingen, San Diego, Calif.), and pFastBac (Life Technologies, Gaithersburg, Md.). The person of ordinary skill in the art would be aware of other vectors suitable for maintenance propagation or expression of the nucleic acid molecules described herein. These are found for example in Sambrook, J., Fritsh, E. F., and Maniatis, T. Molecular Cloning: A Laboratory Manual 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989.

[0144] The invention also encompasses vectors in which the nucleic acid sequences described herein are cloned into the vector in reverse orientation, but operably linked to a regulatory sequence that permits transcription of antisense RNA. Thus, an antisense transcript can be produced to all, or to a portion, of the nucleic acid molecule sequences described herein, including both coding and non-coding regions. Expression of this antisense RNA is subject to each of the parameters described above in relation to expression of the sense RNA (regulatory sequences, constitutive or inducible expression, tissue-specific expression).

[0145] The invention also relates to recombinant host cells containing the vectors described herein. Host cells therefore include prokaryotic cells, lower eukaryotic cells such as yeast, other eukaryotic cells such as insect cells, and higher eukaryotic cells such as mammalian cells. Preferred host cells of the instant invention include E. coli and Sf9.

[0146] The recombinant host cells are prepared by introducing the vector constructs described herein into the cells by techniques readily available to the person of ordinary skill in the art. These include, but are not limited to, calcium phosphate transfection, DEAE-dextran-mediated transfection, cationic lipid-mediated transfection, electroporation, transduction, infection, lipofection, and other techniques, such as those found in Sambrook et al. (Molecular Cloning: A Laboratory Manual. 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989).

[0147] Host cells can contain more than one vector. Thus, different nucleotide sequences can be introduced on different vectors of the same cell. Similarly, the nucleic acid molecules can be introduced either alone or with other nucleic acid molecules that are not related to the nucleic acid molecules such as those providing trans-acting factors for expression vectors. When more than one vector is introduced into a cell, the vectors can be introduced independently, co-introduced or joined to the nucleic acid molecule vector.

[0148] In the case of bacteriophage and viral vectors, these can be introduced into cells as packaged or encapsulated virus by standard procedures for infection and transduction. Viral vectors can be replication-competent or replication-defective. In the case in which viral replication is defective, replication will occur in host cells providing functions that complement the defects.

[0149] Vectors generally include selectable markers that enable the selection of the subpopulation of cells that contain the recombinant vector constructs. The marker can be contained in the same vector that contains the nucleic acid molecules described herein or may be on a separate vector. Markers include tetracycline or ampicillin-resistance genes for prokaryotic host cells and dihydrofolate reductase or neomycin resistance for eukaryotic host cells. However, any marker that provides selection for a phenotypic trait will be effective.

[0150] While the active proteins can be produced in bacteria, yeast, mammalian cells, and other cells under the control of the appropriate regulatory sequences, cell- free transcription and translation systems can also be used to produce these proteins using RNA derived from the DNA constructs described herein.

[0151] Where secretion of the peptide is desired, appropriate secretion signals are incorporated into the vector. The signal sequence can be endogenous to the peptides or heterologous to these peptides.

[0152] It is also understood that depending upon the host cell in recombinant production of the peptides described herein, the peptides can have various glycosylation patterns, depending upon the cell, or maybe non-glycosylated as when produced in bacteria. In addition, the peptides may include an initial modified methionine in some cases as a result of a host-mediated process.

[0153] The recombinant host cells expressing the peptides described herein have a variety of uses. First, the cells are useful for producing a peptide or protein that can be further purified to produce desired amounts of protein or fragments. Thus, host cells containing expression vectors are useful for peptide production.

[0154] Host cells are also useful for conducting cell-based assays involving the ERAB or HADH2 protein/peptide, or its fragments. Thus, a recombinant host cell expressing a native protein is useful for assaying compounds that stimulate or inhibit protein function.

[0155] Host cells are also useful for identifying ERAB or HAHD2 protein mutants in which these functions are affected. If the mutants naturally occur and give rise to a pathology, host cells containing the mutations are useful to assay compounds that have a desired effect on the mutant protein (for example, stimulating or inhibiting function) which may not be indicated by their effect on the native protein.

EXAMPLES

[0156] A. Synthesis of an ERAB or HADH2 Inhibitor (Compound I)

[0157] The structure of Compound I as a single enantiomer is shown in FIG. 4A. Compound I was synthesized using two reaction schemes. The abbreviations employed in the Schemes have the following meaning unless otherwise indicated: Me: methyl; Et: ethyl; Ac: acetyl; Boc: butyloxycarbonyl; EtoAc: ethyl acetate; TFA: trifluoroacetic acid; DCC: dicyclohexylcarbodimide; rt: room temperature; HATU: [O-(7-azabenzotriazol-1-yl)-1,1,3,3-tetra-triethyl-uronium hexafluorophsphate; DMAP: N,N-dimethyl-4-aminopyridine; and DMF: dimethylformamide.

[0158] 1. Preparation of 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone (Compound I) According to Scheme 1.

[0159] 1-a. General Description of Scheme 1.

[0160] 2-Chloro-2-phenyl-acetyl chloride (1) and hexamethyleneimine (2) are reacted in dichloromethane in the presence of triethylamine to afford the intermediate (3). This intermediate (3) is then carried forward and reacted with commercially available 4-mercapto-1H-pyrazolo[3,4-d] pyrimidine (4) to afford a mixture of products Compound I and 14. The two products are separated via column chromatography to yield 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone (Compound I) as the minor and 14 major products respectively. The desired Compound I is further purified via preparatory HPLC to yield the product in>95% purity. Compound I, made according to Scheme 1, when tested against ERAB as described below, exhibited an IC₅₀=88 nM.

[0161] 1-b. Experimental Section to Scheme 1.

[0162] 2-Chloro-2-phenyl-acetyl chloride (1) (2.50 ml, 15.75 mmol) was dissolved in CH₂Cl₂ (50 ml), the mixture was cooled to 0° C., hexamethyleneimine (2) (1.76 ml, 15.75 mmol) was added dropwise, followed by triethylamine (2.19 ml, 15.75 mmol). The resulting mixture containing intermediate (3) was stirred at 0° C. for 15 min followed by warming to room temperature and stirring an additional 60 min. The mixture (3) was then concentrated on a rotary evaporator, the residual oil was taken up in dimethylformamide (DMF) (50 ml), triethylamine (2.19 ml, 15.75 mmol) was added, followed by addition of 4-mercapto-1H-pyrazolo[3,4-d]pyrimidine (4) (2.33 g, 15.44 mmol) in one portion as a solid. The reaction product was warmed to 80° C. and stirred for approximately 17 h. The reaction product was cooled to room temperature, diluted with water, and extracted with EtOAc (3×30 ml), and the combined organics were washed with brine, dried over anhyd. Na₂SO₄, filtered and concentrated to obtain crude products (Compound I and 14). The crude products were purified on silica gel eluting with 30-40-80% ethyl acetate/hexane to yield two products. 3.55 g of the product (14) with the lower R_(f) was isolated as a white solid. The desired compound (0.266 g) with higher R_(f) was obtained as a tan solid. This product was further purified by preparatory HPLC (5-95% CH₃CN/H₂O, 10 min, followed by 95% CH₃CN/H₂O, 0.1% trifluoroacetic acid (TFA), 10 min)). The desired HPLC fractions were combined, diluted with brine (30 ml), 50% aqueous NaHCO₃ solution (30 ml) was added, and the aqueous layer extracted with EtOAc (3×30 ml), combined organics washed with brine, dried over anhyd. Na₂SO₄, filtered and concentrated to yield (0.178 g, 0.484 mmol)>95% purity of Compound I. mp: 201-202° C.; R_(f)=0.60 (EtOAc:Hexanes=6:4). ¹H-NMR; (DMSO-d6) δ14.18 (s, 1H), 8.27 (s, 1H), 8.17 (s, 1H), 7.95 (s, 1H), 7.52-7.54 (m, 3H), 7.39-7.41 (m, 2H), 3.19-3.74 (m, 4H), 1.34-1.90 (m, 8H). Anal. Calcd for C₁₉H₂₁N₅OS.0.2 TFA.0.4 H₂O: C, 62.10; H, 5.76; N, 19.06. Found: C, 58.59; H, 5.53; N, 17.84; MALDI HRMS Calcd for C₁₉H₂₁N₅OS (M+H)=368.1545, observed (M+H)=368.1535; HPLC: 10% CH₃CN/H₂O (0.1% TFA)-90% CH₃CN/H₂O (0.1%TFA): Retention time=13.80 min.

[0163] 2. Preparation of 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone (Compound I) according to Scheme 2.

[0164] added dropwise, followed by triethylamine (2.19 ml, 15.75 mmol). The resulting mixture containing intermediate (3) was stirred at 0° C. for 15 min followed by warming to room temperature and stirring an additional 60 min. The mixture (3) was then concentrated on a rotary evaporator, the residual oil was taken up in dimethylformamide (DMF) (50 ml), triethylamine (2.19 ml, 15.75 mmol) was added, followed by addition of 4-mercapto-1H-pyrazolo[3,4-d] pyrimidine (4) (2.33 g, 15.44 mmol) in one portion as a solid. The reaction product was warmed to 80° C. and stirred for approximately 17 h. The reaction product was cooled to room temperature, diluted with water, and extracted with EtOAc (3×30 ml), and the combined organics were washed with brine, dried over anhyd. Na₂SO₄, filtered and concentrated to obtain crude products (Compound I and 14). The crude products were purified on silica gel eluting with 30-40-80% ethyl acetate/hexane to yield two products. 3.55 g of the product (14) with the lower R_(f) was isolated as a white solid. The desired compound (0.266 g) with higher R_(f) was obtained as a tan solid. This product was further purified by preparatory HPLC (5-95% CH₃CN/H₂O, 10 min, followed by 95% CH₃CN/H₂O, 0.1% trifluoroacetic acid (TFA), 10 min)). The desired HPLC fractions were combined, diluted with brine (30 ml), 50% aqueous NaHCO₃ solution (30 ml) was added, and the aqueous layer extracted with EtOAc (3×30 ml), combined organics washed with brine, dried over anhyd. Na₂SO₄, filtered and concentrated to yield (0.178 g, 0.484 mmol)>95% purity of Compound I. mp: 201-202° C.; R_(f)=0.60 (EtOAc:Hexanes=6:4). ¹H-NMR; (DMSO-d6) δ14.18 (s, 1H), 8.27 (s, 1H), 8.17 (s, 1H), 7.95 (s, 1H), 7.52-7.54 (m, 3H), 7.39-7.41 (m, 2H), 3.19-3.74 (m, 4H), 1.34-1.90 (m, 8H). Anal. Calcd for C₁₉H₂₁N₅OS.0.2 TFA.0.4 H₂O: C, 62.10; H, 5.76; N, 19.06. Found: C, 58.59; H, 5.53; N, 17.84; MALDI HRMS Calcd for C₁₉H₂₁N₅OS (M+H)=368.1545, observed (M+H)=368.1535; HPLC: 10% CH₃CN/H₂O (0.1%TFA)-90% CH₃CN/H₂O (0.1% TFA): Retention time=13.80 min.

[0165] 2. Preparation of 1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone (Compound I) according to Scheme 2.

[0166] 2-a. General Description of Scheme 2.

[0167] Boc-L-α-phenylglycine (5) and cyclohexanol are reacted in dichloromethane in the presence of dicyclohexylcarbodiimide (DCC) and catalytic amount of N,N-dimethyl-4-aminopyridine (DMAP) to give 6 (R=Boc) in almost quantitative yield. Treatment of 6 with trifluoroacetic acid (TFA) yields 7 (R=H) in 98% yield. 7 is then coupled to alpha-cyanoacetic acid (8) using O-(7-azabenzotriazol-1-yl)-1,1,3,3-tetra-triethyl-uronium hexafluorophosphate (HATU) as the coupling agent to afford (2-cyano-acetylamino)-phenyl-acetic acid cyclohexyl ester (9). The reaction of 9 with triethyl orthoformate in acetic anhydride and catalytic anhydrous ZnCl₂ gives an intermediate which upon reaction with hydrazine in 1,4-dioxane at 105° C. affords 10 in 51% yield. The [(5-amino-1H-pyrazol-4-carbonyl)-amino]-phenyl-acetic acid cyclohexyl ester (10) is then treated with formamide at 180-100° C. to give the desired cyclized product (11). Compound 11 is treated with Lawesson's reagent under inert gas atmosphere to afford compound 12. Hydrolysis of compound 12 affords the carboxylic acid 13, which is then coupled to hexamethyeneimine using the coupling reagent HATU to afford Compound I.

[0168] 2-b. Experimental Section to Scheme 2.

[0169] Step 1: tert-Butoxycarbonylamino-phenyl-acetic Acid Cyclohexyl Ester (6).

[0170] To an ice-cold suspension of Boc-L-α-phenylglycine (5) (14.14 g, 40.35 mmol) and DMAP (0.5 g, 4.04 mmol) and cyclohexanol (5.12 ml, 48.42 mmol) in 60 ml of CH₂Cl₂ was slowly added DCC (9.16 g, 44.4 mmol). The resulting mixture was stirred at 0° C. to room temperature and monitored by TLC. Upon completion the reaction was filtered and the precipitate was washed with CH₂Cl₂ to remove most of the N,N′-dicyclohexylurea. The filtrate was then partitioned between CH₂Cl₂ and satd. NaHCO₃ and the layers separated. The aqueous phase was extracted with CH₂Cl₂ (2×200 ml), and the combined organics were washed with H₂O (150 ml), brine (150 ml) and dried over anhyd. Na₂SO₄, filtered, and concentrated under reduced pressure. The resulting yellowish oil was chromatographed on silica gel using Hexane:EtOAc=2:1 as the elutant to yield compound 6 (13.37 g, 39.95 mmol, 99% yield) as a viscous yellow oil. TLC; R_(f)=0.7 (EtOAc:Hexanes=6:4). ¹H-NMR; (CDCl₃) δ1.27-1.83 (m, 10H), 1.47 (s, 9H) 4.78-4.83 (m, 1H), 5.31-5.33 (d, 1H, J=8 Hz), 5.61-5.63 (br, s, 1H, NH), 7.32-7.41 (m, 5H). MS Calcd for C₁₉H₂₇NO₄ (M+H)=334, observed (M+H)=334; HPLC: 30% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA)/20 min: Retention time=14.61 min.

[0171] Step 2: Amino-phenyl-acetic Acid Cyclohexyl Ester (7).

[0172] To a solution of 6 (13.27 g, 39.79 mmol) in 50 ml of CH₂Cl₂ at 0° C. was added TFA (30 ml, 385.1 mmol) dropwise. The resulting yellowish mixture was stirred at 0° C. to room temperature overnight. The reaction was then concentrated under reduced pressure and the resulting yellow oil was partitioned between CH₂Cl₂ (300 ml) and satd. NaHCO₃ (150 ml) and the layers separated. The aqueous phase was extracted with CH₂Cl₂ (2×150 ml) and the combined organics were washed with H₂O (150 ml), brine (150 ml) and dried over anhyd. Na₂SO₄, filtered and concentrated under reduced pressure to yield compound 7 (9.05 g, 38.99 mmol, 98% yield) as a yellow oil. TLC; R_(f)=0.7 (CH₂Cl₂:MeOH=9:1).¹H-NMR (CDCl₃) δ1.25-2.03 (m, 10H), 4.62 (s, 1H), 4.81-4.85 (m, 1H), 7.30-7.43 (m, 5H). MS Calcd for C₁₄H₁₉NO₂ (M+H)=334, observed (M+H)=334; HPLC: 5% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA)/20min. Retention time=7.52 min.

[0173] Step 3: (2-Cyano-acetylamino)-phenyl-acetic Acid Cyclohexyl Ester (9).

[0174] To a solution of 7 (9.01 g, 38.63 mmol), α-cyanoacetic acid (8) (3.58 g, 42.05 mmol) and triethylamine (12 ml, 84.1 mmol) in 60 ml of DMF at 0° C. was added HATU (24 g, 63.1 mmol). The yellow solution was stirred at 0° C. to room temperature overnight. The reaction was then partitioned between EtOAc (300 ml) and H₂O (150 ml) and the layers separated. The organic phase was washed with satd. NaHCO₃ (150 ml), H₂O (150 ml), 0.5 N HCl (150 ml), brine (150 ml), and dried over anhyd. Na₂SO₄, filtered and concentrated under reduced pressure. The resulting yellow oil was chromatographed on silica gel using hexane:EtOAc=1:1 as the elutant to yield compound 9 (6.57 g, 21.88 mmol, 57% yield) as a white solid. mp: 114-116° C.; TLC; R_(f)=0.8 (EtOAc:Hexanes=1:1). ¹H-NMR; (CDCl₃) δ1.28-1.85 (m, 10H), 3.45 (s, 2H), 4.87-5.00 (m, 1H), 5.54-5.56 (d, 1H, J=7 Hz), 7.10-7.29 (br, s, 1H, NH), 7.29-7.39 (s, 5H). MS Calcd for C₁₇H₂₀N₂O₃ (M+Na)=323, observed (M+Na)=323, observed (M+Na)=323; HPLC:30% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA)/20min. Retention time=9.67 min.

[0175] Step 4: (5Amino-1H-pyrazol-4-carbonyl)-aminol-phenyl-acetic Acid Cyclohexyl Ester (10)

[0176] A round-bottom flask was charged with compound 9 (2.3 g, 7.67 mmol), triethyl orthoformate (9.0 ml, 53.7 mmol), acetic anhydride (4.5 ml, 46.02 mmol), and anhyd. ZnCl₂ (1.05 g, 7.67 mmol), and then heated to reflux at 130° C. for 4 h, most preferably 105° C. for 4 h. The yellow reaction mixture was concentrated under vacuum and azeotroped with toluene (3×15 ml). The resulting was titrated with CH₂Cl₂ (100 ml) filtered and washed with CH₂Cl₂ (150 ml). The filtrate was then concentrated under vacuum to yield crude residue as yellow grease. The crude residue was treated with hydrazine hydrate (0.56 ml, 11.51 mmol) in 10 ml of 1,4-dioxane and then refluxed at 105° C. overnight. The reaction was cooled to room temperature and concentrated under vacuum. The residue was partitioned between EtOAc (250 ml) and satd. NaHCO₃, brine (2×100 ml), dried over anhyd. Na₂SO₄, filtered and concentrated under vacuum to afford the crude product as a yellow grease. The crude product was chromatographed using silica gel and eluted with CH₂Cl₂:MeOH=9:1 to afford compound 10 (1.343 g, 3.92 mmol, 51% yield) as a white solid. mp: 92-94° C.; TLC; R_(f)=0.4 (CH₂Cl₂:MeOH=9:1). ¹H-NMR; (CDCl₃/CD₃OD) δ1.14-1.37 (m, 4H), 1.38-1.41 (m, 2H), 1.52-1.54 (m, 2H); 1.67-1.71 (m, 2H), 4.68-4.72 (m,1H), 5.53 (s, 1H), 7.29-7.30 (m, 5H), 7.79 (s, 1H). MS Calcd for C₁₈H₂₂N₄O₃ (M+H)=343, observed (M+H)=343; 5% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA)/20min. Retention time=9.24 min.

[0177] Step 5: (4-Oxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-phenyl-acetic Acid Cyclohexyl Ester (11).

[0178] Compound 10 (1.244 g, 3.63 mmol) in 8 ml of formamide was heated to 180° C. for 4 h and then at 100° C. overnight, most preferably 145° overnight. The cooled reaction was filtered and the white precipitate product (11) was washed with and dried in a vacuum oven over P₂O₅. Additionally, the filtrate was concentrated under reduced pressure and the residue was partitioned between EtOAc (250 ml) and satd. NaHCO₃ (2×100 ml), wash with brine (100 ml), dried over anhyd. Na₂SO₄, filtered and concentrated under vacuum to afford the crude product as a yellow grease, which was then chromatographed using silica gel and eluted with CH₂Cl₂:EtOAc (1:1) to afford an additional 0.341 g, 0.97 mmol, and 27% of compound 11 as a white solid. mp: 176-180° C.; TLC; R_(f)=0.5 (CH₂Cl₂:EtOAc=1:1). ¹H-NMR; (CDCl₃) δ1.24-1.91 (m, 10H), 4.98-5.03 (m, 1H), 6.84 (s, 1H), 7.29-7.30 (m, 2H), 7.36-7.49 (m, 3H), 7.91 (s, 1H), 8.23 (s, 1H). MS Calcd for C₁₉H₂₀N₄O₃ (M+H)=353, observed (M+H)=353; HPLC:5% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA)/20min. Retention time=12.9 min.

[0179] Step 6: 2-Phenyl-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-acetic Acid Cyclohexyl Ester (12).

[0180] A solution of compound 11 (0.326 g, 0.93 mmol) in 5 ml of xylene was purged with argon for 20 minutes, to which was then added Lawesson's reagent (0.375 g, 0.93 mmol) and the resulting mixture heated at 145° C. for 2 h under argon. The yellow reaction mixture was concentrated under vacuum and partitioned between EtOAc (100 ml) and satd. NaHCO₃, washed with brine (2×50 ml), dried over anhyd. Na₂SO₄, filtered and concentrated under vacuum. The crude product was chromatographed using silica gel and eluted with CH₂Cl₂:EtOAc (1:1) to afford 0.316 g, 0.86 mmol, 92% yield of product 12 as a off white solid. mp: 170-173° C.; TLC: R_(f)=0.8 (CH₂Cl₂:EtOAc=1:1). ¹H-NMR (CDCl₃) δ1.30-1.93 (m, 10H), 5.03 (m, 1H), 7.41-7.49 (m, 5H), 7.98 (s, 1H), 8.04 (s, 1H), 8.38 (s, 1H), 10.55 (br, s, 1H, NH). MS Calcd for C₁₉H₂₀N₄O₂S (M+H)=368, observed (M+H)=369; HPLC:5% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA)/20min. Retention time=14.6 min.

[0181] Step 7: 2-Phenyl-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)acetic Acid (13).

[0182] To a solution of 2-phenyl-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)acetic acid cyclohexyl ester (12), 0.467 g, 1.27 mmol, in 10 ml of methanol was added to 2N KOH aqueous solution (1.3 ml, 2.53 mmol) at 0° C. The resulting mixture of yellow solution was stirred at 0° C. to room temperature overnight. The reaction mixture was concentrated by vacuum to remove most of methanol and water was added. The pH was adjusted to 4.0 with aqueous 10% citric acid solution. The product was extracted with EtOAc (2×75 ml). The combined organic layer was washed with water, brine and dried over anhyd. Na₂SO₄, then concentrated by vacuum to afford compound 13 (0.354 g, 1.19 mmol, 97% yield) as an off-white solid. mp: 95-98° C.; TLC; R_(f)=0.1 (CH₂Cl₂:MeOH=9:1). ¹H-NMR; (CD₃OD) δ3.23 (s, 1H), 7.50 (s, 5H), 8.08 (s, 1H), 8.09 (s, 1H), 8.34 (s, 1H, NH). MS Calcd for C₁₃H₁₀N₄O₂S (M+H)=287, observed (M+H)=287; HPLC:5% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA)/20min. Retention time=3.9 min.

[0183] Step 8: 1-Azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-1,4-dihrdropyrazolo [3,4-d]pyrimidin-5-yl)-ethanone (Compound I).

[0184] To a solution of 2-phenyl-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)acetic Acid (13), 0.064 g, 0.22 mmol, and hexamethyleneimine (0.023 g, 0.23 mmol) with 4-methylmorpholine (50 μl, 0.44 mol) in 3 ml of DMF at 0° C. was added HATU [O-(7-azabenzotriazol-1-yl)-1,1,3,3-tetra-triethyl-uronium hexafluorophosphate] (0.125 g, 0.33 mol). The resulting mixture of yellow solution was stirred at 0° C. to room temperature for overnight. The yellow reaction mixture was partitioned between EtOAc (100 ml) and brine, satd. NaHCO₃, brine (3×50 ml). The organic layer dried over anhyd. Na₂SO₄, filtered and concentrated under vacuum. The crude product was chomatographed using silica gel and eluted with CH₂Cl₂:EtOAc (1:1) to afford Compound I (0.043 g, 0.12 mmol, 53% yield) as a yellowish solid. The Compound I obtained via the above procedure appears to be a different crystalline form from that obtained via Scheme 1. This may account for the different melting points. Co-injection of Compound I obtained via step 8, Scheme 2 and that from Scheme 1 gave a single peak via HPLC. mp:>230° C. TLC; R_(f)=0.7 (CH₂Cl₂:EtOAc=1:1). ¹H-NMR; (CDCl₃) δ1.60-2.08 (m, 8H), 3.37-3.84 (m, 4H), 7.44-7.49 (m, 5H), 8.09 (s, 1H), 8.36 (s, 1H), 8.41 (s, 1H), 10.65 (s, br, 1H, NH). MS Calcd for C₁₉H₂₁N₅OS (M+H)=368, observed (M+H)=368; HPLC:5% CH₃CN/H₂O (0.1% TFA) to 90% CH₃CN/H₂O (0.1% TFA)/20min. Retention time=11.66 min.

[0185] B. Cloning, Overexpression, and Purification of Wild Type and Mutant Peptides of ERAB or HADH2.

[0186] The coding sequence for full length wild-type ERAB or HADH2 [SEQ ID NO: 7, Yan et al., (1997), supra; He et al., (1998), supra] was amplified by PCR [Mullis et al., Cold Spring Harbor Symposium Quantum Biology, Vol. 51, pp. 263 -273 (1986); Saiki et al., Science, Vol. 239, pp. 487-491 (1988)] from a Marathon-Ready human lung cDNA library and the Advantage™ cDNA PCR kit, both from Clontech (Palo Alto, Calif.), using the manufacturer's instructions. The forward primer was 5′-GGGCACACCATGGCAGCAGCGTGTCGGAGCGTGAAGG-3′ (SEQ ID NO: 9) and the reverse primer was 5 ′-AGCTTTCGGCCGTTAAGGCTGCATACGAATAGCCCCATCC-3′ (SEQ ID NO: 10).

[0187] The amplified DNA was digested with the restriction enzymes NcoI and Eagl, ligated into the E. coli plasmid pMGH4 [Kan et al., Journal of Protein Chemistry, Vol. 11, pp. 467-473 (1992); Schoner et al., Proceedings of National Academy of Science, USA, Vol. 83, pp. 8506-8510 (1986)], sequence verified, and compared to the sequences in GENBANK Accession numbers AF035555 and U96132.

[0188] Mutations were introduced by oligonucleotide site-directed mutagenesis [Kunkel, Proceedings of National Academy of Science, USA, Vol. 82, pp. 488-492 (1985)] using the Muta-Gene in vitro Mutagenesis Kit (obtained from Bio-rad, Hercules, Calif.). The ssDNA uracil template (minus strand) was created in E. coli strain CJ236 supplied in the kit using the pMGH4-ERAB or HADH2 construct. All DNA modification and restriction enzymes were purchased from New England Biolabs and oligonucleotides were purchased from Genosys Biotechnology.

[0189] The following oligonucleotides were used for mutagenesis: C5V 5′-CCATGGCAGCAGCTGTTCGGAGCGTGAAGG-3′ (SEQ ID NO:11) C58V 5′-GAAGTTAGGAAACAACGTTGTTTTCGCCCCAGCC-3′ (SEQ ID NO:12) C214R 5′-CCAGAGAAAGTGCGTAACTTCTTAGCCAGCCAAG-3′ (SEQ ID NO:13) C124A 5′-CCAGAGAAAGTAGCAAACTTCCTCGCCAGCCAAG-3′ (SEQ ID NO:21) C214S 5′-CCAGAGAAAGTGTCTAACTTCTTAGCCAGCCAAG-3′ (SEQ ID NO:24)

[0190] All mutants were sequence-verified through the region of the mutations and tested for expression in a spontaneous mutant of E. coli strain B121 (DE3) (obtained from Novagen, Madison, Wis.) [See Miroux et al., Journal of Molecular Biology, Vol. 260, pp. 289-298 (1996)].

[0191] Wild-type and mutant proteins were purified in the same manner. The final purification protocol was modified from published reports [Furuta et al., Biochemistry Biophysics Acta, Vol. 1350, pp. 317-324 (1997)]. All procedures were carried out at 4° C. Cell paste was resuspended in half volume 50 mM Tris-HCl pH 7.5, 1 mM EDTA, 10 mM β-mercaptoethanol (BME). The cells were disrupted by micro-fluidization. Cleared supernatant was passed through a Q-Sepharose Fast Flow column. Unbound enzyme was collected in the flow through. This was loaded directly onto a Blue Sepharose Fast Flow column equilibrated in 20 mM Tris-HCl pH 7.5, 10 mM BME, 0.01% NaN₃. ERAB or HADH2 was eluted with a salt gradient increasing to 1 M NaCl over 10 column volumes. Peak fractions were concentrated for size exclusion. The pool was fractionated on a 500 ml Superdex 200 column equilibrated in 20 mM Tris-HCl pH 7.5, 200 mM NaCl, 5-10 mM BME, 0.01% NaN₃. The peak eluted as a tetramer. The peak fractions were concentrated to 20-25 mg/ml and stored in aliquots at −20° C. All chromatography media were from Pharmacia Biotech.

[0192] C. Isothermal Titration Calorimetry

[0193] Titrations described herein were performed with an MCS microcalorimeter (obtained from MicroCal, Inc., Northampton, Miss.).

[0194] For the inhibitor binding experiments, the titrations were performed in 25 mM MOPS (pH 7.5), 125 mM NaCl, 10% glycerol, 2.0% DMSO, 0.5 mM TCEP (Tri(2-carboxyethyl)phosphine), 0.1 mM EDTA at 15° C. The syringe contained 415 μM wild-type ERAB or HADH2 and the cell contained either 20 μM inhibitor, 20 μM cofactor, or 20 μM each of inhibitor and cofactor. After a preliminary 20 μL injection, 12 injections of 10.0 μL each were made at 4 minute intervals. Dilution control titrations of buffer into buffer, protein into buffer, and buffer into inhibitor, cofactor and inhibitor/cofactor mixture were also performed. For the cofactor binding experiments, the titrations were performed in 50 mM MOPS (3-(N-morpholino) propanesulfonic acid, pH 7.5), 250 mM NaCl, 10% glycerol, 2.0% DMSO, 10 mM TCEP at 15° C.

[0195] For the NADH titration, the syringe contained 700 μM cofactor and the cell contained 35 μM wild type ERAB or HADH2. For the NAD⁺ titration, the syringe contained 2.68 mM cofactor and the cell contained 127 μM wild-type ERAB or HADH2.

[0196] The IC₅₀ value for Compound I was determined spectrophotometrically by monitoring the reduction of NADH to NAD⁺ with acetoacetyl-CoA as substrate. Enzyme (2.5 nM) was preincubated with inhibitor for 400 seconds at 30° C. in the presence of 36 uM NADH, 25 mM MOPS, pH 7.5, 250 mM NaCl, 2% (v/v) DMSO, and 2.5 mM TCEP. The reaction was initiated by addition of substrate (38 μM). Reduction of NADH was monitored at 340 λ. The IC₅₀ value was determined by non-linear regression analysis using KaleidaGraph (obtained from Synergy Software, Reading, Pa.).

[0197] Compound I made according to Scheme 2 was found to have an average IC₅₀ of 92±5 nM against ERAB or HADH2 (for a racemic mixture of the compound). The experimental data and co-crystal structure of the compound indicates that Compound I inhibits the ERAB or HADH2 via an interaction with NAD⁺, which is the natural co-factor for ERAB or HADH2. This interaction with NAD⁺ enables Compound I to bind ERAB or HADH2, approximately 1000-fold more potently than in the absence of NAD⁺. Further, the tertiary structure analysis of the crystallized ERAB or HADH2:inhibitor complex shows that the inhibitor binds in the active site cavity of the enzyme and reacts with the NAD⁺ cofactor to form a covalent adduct (FIG. 4C). The conformation and binding interactions of the inhibitor appear identical in the three ERAB or HADH2 monomers to which it binds in the crystal.

[0198] Referring to FIGS. 4A and 4C, the N2 nitrogen of the inhibitor is covalently linked to the reactive C4 carbon on the nicotinamide ring of the NAD⁺. Adduct formation does not alter the conformation of the bound NAD⁺ cofactor beyond movement of the C4 atom out of the plane of the nicotinamide ring. Consistent with the observed covalent binding, experiments using isothermal titration calorimetry demonstrate that the inhibitor binds weakly to ERAB or HADH2 in the absence of cofactor or in the presence of NADH (FIG. 5). No binding was detected when ERAB or HADH2 was titrated into either inhibitor or NAD⁺ alone. A reaction was detected, however, when ERAB or HADH2 was titrated into an equimolar mixture of inhibitor and NAD⁺. The data display the characteristics of a tight-binding curve involving one mole of ERAB or HADH2 per mole of inhibitor/NAD⁺ mixture. The results obtained when ERAB or HADH2 was titrated into an equimolar mixture of inhibitor and NADH, on the other hand, are comparable to the results obtained when the protein was titrated into NADH alone. Similar results were observed using the C214R mutant of ERAB or HADH2. This observed reaction cannot simply be attributed to NAD⁺ binding to ERAB or HADH2, as the Kd for NAD⁺ was independently determined to be on the order of 500 uM. Therefore, a high cooperative binding of NAD⁺ and inhibitor must account for the observed reaction. No significant cooperativity was observed for NADH binding in the presence of inhibitor. The formation of a covalent adduct apparently occurs because the inhibitor closely mimics the reaction stereochemistry of the substrate. A proposed mechanism for the reaction of Compound I with NAD⁺ is shown in FIG. 4C.

[0199] Despite a lack of structural similarity between Compound I and either of the ERAB or HADH2 substrates (wild-type or mutant ), the inhibitor is in intimate contact with the protein within the substrate-binding cleft. A schematic representation of the protein-ligand interactions is shown in FIG. 4D. The inhibitor contacts nine protein residues, primarily through hydrophobic interactions. Two hydrogen bonds are formed between Compound I and ERAB or HADH2, one between the OH of Tyr 168 and N1 of Compound I and the other between N_(ε) of Gln 165 and the carbonyl oxygen of Compound I. As mentioned previously, human 17β-hydroxysteroid dehydrogenase is a human protein closely related to ERAB or HADH2 whose structure has been reported (Ghosh et al., Structure, Vol. 3, pp. 503-513 (1995)). Likewise, 15-PGD and CAA20237.1, identified using the BLAST search engine (Altschul et al., Nucleic Acids Research, Vol. 25, pp. 3389-3402 (1997)), are two reported human sequences closely related to ERAB or HADH2 (see FIG. 2). At most three of the nine residues that interact with the inhibitor are found in any of these three related proteins. This uniqueness suggests that a high level of specificity may be attainable for ERAB or HADH2 inhibitors. Consistent with this, Compound I showed no detectable inhibition of two closely related members of the SDR family, E. coli 17β-hydroxysteroid dehydrogenase and Streptomycetes hydrogenans 3α-20β- hydroxysteroid dehydrogenase, at concentrations as high as 100 μM.

[0200] D. Crystallographic Analysis

[0201] The C214R mutant of ERAB or HADH2, made by the mutagenesis process described above, was engineered to avoid cysteine oxidation in the protein, with arginine selected as the replacement amino acid because of its occurrence at this position in other mammalian ERAB or HADH2 sequences (He et al., Journal of Biochemistry Vol. 273, pp. 10741-10746 (1998)). The C214R mutant of ERAB or HADH2 was concentrated to 20 mg/ml for crystallization. Five mM β-NAD and 5 mM Compound I were combined; and the precipitate removed by centrifugation. Initial thin plates were observed in Hampton Crystal Screen condition 40 (20% isopropanol, 20% PEG 4000, pH 5.6). The final conditions for crystal growth were 20% MME PEG 2000, 0.1 M Na citrate pH 6.0, 4% isopropanol. Nuclei were introduced to the drops by streak seeding [Stura et al., Journal of Crystal Growth, Vol. 110, pp. 270-282 (1991)]. Single, thick plates grew over five days. Isopropanol, Tris, EDTA, glycerol and sodium citrate were all purchased from Fisher Scientific (Pittsburgh, Pa.). NaCl, β-mercaptoethanol, acetyl CoA, β-NAD⁺ and MME PEG 2000 were from Sigma. PEG 400 was from BDH Laboratory Supplies (Poole, England). Crystal Screen and VDX plates were purchased from Hampton Research (Laguna Niguel, Calif.).

[0202] The results from the crystallographic analysis are shown in Table I below. Crystal coordinates are set forth in Table II. TABLE I Data Collection, Molecular Replacement, and Refinement Statistics Crystal Information Space group C2 Unit cell parameters a = 122.0 Å, b = 80.8 Å, c = 110.0 Å, β = 105.6° Estimated solvent content    50% Data Collection Resolution 30.0-2.0 Å Total observations 221,823 Unique reflections (completeness)  69,169 (99.4%) Rsym     0.066 Molecular Replacement Program EPMR Data resolution range 15.0-4.0 Å Solution correlation coefficient/R-factor     0.682/0.361 Refinement Resolution range 25.0-2.0 Å Number of reflections   68595 Final R-factor (R-free)     0.215 (0.263) Number of non-hydrogen atoms Protein   7224 NAD    176 Compound I    78 Water    282 Rms deviations from ideal geometry Bond lengths     0.005 Å Bond angles     1.5° Residues within most favored    91.9% regions of Ramachandran plot

[0203] TABLE II Crystal coordinates of the ERAB or the HADH22:Compound I complex ATOM 1 CB SER A 7 51.735 12.841 30.482 1.000 22.48 ATOM 2 C SER A 7 53.935 12.748 29.330 1.000 44.59 ATOM 3 O SER A 7 53.965 12.623 28.111 1.000 43.24 ATOM 4 N SER A 7 52.577 14.801 29.231 1.000 59.99 ATOM 5 CA SER A 7 52.952 13.663 30.055 1.000 50.69 ATOM 6 N VAL A 8 54.749 12.075 30.131 1.000 39.56 ATOM 7 CA VAL A 8 55.600 11.010 29.608 1.000 36.12 ATOM 8 CB VAL A 8 56.868 10.859 30.460 1.000 38.89 ATOM 9 CG1 VAL A 8 57.743 12.106 30.341 1.000 32.22 ATOM 10 CG2 VAL A 8 56.501 10.596 31.916 1.000 29.19 ATOM 11 C VAL A 8 54.816 9.703 29.573 1.000 31.85 ATOM 12 O VAL A 8 55.319 8.694 29.085 1.000 33.39 ATOM 13 N LYS A 9 53.585 9.748 30.085 1.000 39.60 ATOM 14 CA LYS A 9 52.728 8.572 30.162 1.000 29.90 ATOM 15 CB LYS A 9 51.315 8.942 30.592 1.000 28.88 ATOM 16 C LYS A 9 52.675 7.826 28.833 1.000 31.95 ATOM 17 O LYS A 9 52.345 8.403 27.798 1.000 32.99 ATOM 18 N GLY A 10 53.024 6.543 28.880 1.000 33.00 ATOM 19 CA GLY A 10 53.013 5.713 27.696 1.000 32.38 ATOM 20 C GLY A 10 54.267 5.765 26.855 1.000 33.35 ATOM 21 O GLY A 10 54.439 4.954 25.937 1.000 38.54 ATOM 22 N LEU A 11 55.173 6.706 27.127 1.000 29.52 ATOM 23 CA LEU A 11 56.388 6.795 26.319 1.000 36.56 ATOM 24 CB LEU A 11 57.087 8.136 26.562 1.000 27.30 ATOM 25 CG LEU A 11 56.273 9.399 26.270 1.000 34.09 ATOM 26 CD1 LEU A 11 57.138 10.635 26.489 1.000 37.47 ATOM 27 CD2 LEU A 11 55.701 9.388 24.860 1.000 30.46 ATOM 28 C LEU A 11 57.340 5.641 26.619 1.000 25.91 ATOM 29 O LEU A 11 57.359 5.140 27.744 1.000 25.89 ATOM 30 N VAL A 12 58.113 5.236 25.611 1.000 24.21 ATOM 31 CA VAL A 12 59.120 4.198 25.754 1.000 24.85 ATOM 32 CB VAL A 12 59.025 3.133 26.644 1.000 27.51 ATOM 33 CG1 VAL A 12 60.027 2.022 24.931 1.000 23.67 ATOM 34 CG2 VAL A 12 57.620 2.569 24.502 1.000 27.54 ATOM 35 C VAL A 12 60.533 4.781 25.713 1.000 29.72 ATOM 36 O VAL A 12 60.961 5.327 24.691 1.000 28.03 ATOM 37 N ALA A 13 61.284 4.665 26.808 1.000 27.51 ATOM 38 CA ALA A 13 62.633 5.221 26.840 1.000 25.01 ATOM 39 CB ALA A 13 62.764 6.230 27.972 1.000 23.55 ATOM 40 C ALA A 13 63.709 4.156 26.996 1.000 26.59 ATOM 41 O ALA A 13 53.678 3.310 27.887 1.000 29.37 ATOM 42 N VAL A 14 64.702 4.209 26.111 1.000 22.79 ATOM 43 CA VAL A 14 65.894 3.371 26.286 1.000 23.38 ATOM 44 CB VAL A 14 66.418 2.828 24.955 1.000 24.29 ATOM 45 CG1 VAL A 14 67.737 2.093 25.113 1.000 22.79 ATOM 46 CG2 VAL A 14 65.376 1.889 24.355 1.000 24.04 ATOM 47 C VAL A 14 66.940 4.213 27.012 1.000 27.20 ATOM 48 O VAL A 14 67.350 5.258 26.513 1.000 25.93 ATOM 49 N ILE A 15 67.326 3.763 28.196 1.000 24.90 ATOM 50 CA ILE A 15 68.260 4.512 29.039 1.000 22.39 ATOM 51 CB ILE A 15 67.608 4.791 30.408 1.000 25.05 ATOM 52 CG2 ILE A 15 68.514 5.626 31.295 1.000 24.50 ATOM 53 CG1 ILE A 15 66.225 5.437 30.298 1.000 26.19 ATOM 54 CD1 ILE A 15 65.483 5.627 31.601 1.000 29.49 ATOM 55 C ILE A 15 69.566 3.752 29.192 1.000 23.74 ATOM 56 O ILE A 15 69.630 2.729 29.877 1.000 22.94 ATOM 57 N THR A 16 70.629 4.224 28.535 1.000 23.34 ATOM 58 CA THR A 16 71.921 3.555 28.681 1.000 22.89 ATOM 59 CB THR A 16 72.884 3.870 27.258 1.000 21.08 ATOM 60 OG1 THR A 16 73.546 5.110 27.809 1.000 22.39 ATOM 61 CG2 THR A 16 72.116 4.034 26.222 1.000 18.21 ATOM 62 C THR A 16 72.563 3.962 30.006 1.000 18.37 ATOM 63 O THR A 16 72.328 5.085 30.456 1.000 22.95 ATOM 64 N GLY A 17 73.338 3.053 30.591 1.000 22.86 ATOM 65 CA GLY A 17 73.856 3.305 31.939 1.000 22.89 ATOM 66 C GLY A 17 72.716 3.236 32.947 1.000 26.28 ATOM 67 O GLY A 17 72.844 3.705 37.080 1.000 24.11 ATOM 68 N GLY A 17 71.589 2.647 32.543 1.000 24.25 ATOM 69 CA GLY A 17 70.398 2.613 33.367 1.000 22.22 ATOM 70 C GLY A 17 70.476 1.749 34.607 1.000 23.39 ATOM 71 O GLY A 17 69.530 1.757 35.401 1.000 25.11 ATOM 72 N ALA A 19 71.533 0.981 34.851 1.000 22.33 ATOM 73 CA ALA A 19 71.533 0.130 36.042 1.000 23.45 ATOM 74 CB ALA A 19 72.441 −1.094 35.839 1.000 20.63 ATOM 75 C ALA A 19 72.023 0.898 37.269 1.000 29.15 ATOM 76 O ALA A 19 71.941 0.421 38.399 1.000 28.79 ATOM 77 N SER A 20 72.534 2.110 37.069 1.000 25.73 ATOM 78 CA SER A 20 73.135 2.829 38.192 1.000 24.12 ATOM 79 CB SER A 20 74.627 2.487 38.237 1.000 25.36 ATOM 80 OG SER A 20 75.308 3.189 39.253 1.000 28.39 ATOM 81 C SER A 20 72.923 4.333 38.087 1.000 27.60 ATOM 82 O SER A 20 72.555 4.843 37.025 1.000 25.39 ATOM 83 N GLY A 21 73.151 5.015 39.199 1.000 25.28 ATOM 84 CA GLY A 21 73.234 6.445 39.322 1.000 23.93 ATOM 85 C GLY A 21 72.214 7.255 38.556 1.000 27.30 ATOM 86 O GLY A 21 71.002 7.148 38.761 1.000 21.90 ATOM 87 N LEU A 22 72.670 8.121 37.652 1.000 23.35 ATOM 88 CA LEU A 22 71.727 9.032 36.990 1.000 22.33 ATOM 89 CB LEU A 22 72.489 10.123 36.238 1.000 22.48 ATOM 90 CG LEU A 22 73.530 10.891 37.065 1.000 20.02 ATOM 91 CD1 LEU A 22 74.242 11.934 36.220 1.000 17.51 ATOM 92 CD2 LEU A 22 72.873 11.552 38.269 1.000 19.27 ATOM 93 C LEU A 22 70.776 8.278 36.072 1.000 21.31 ATOM 94 O LEU A 22 69.584 8.600 36.033 1.000 25.91 ATOM 95 N GLY A 23 71.281 7.281 35.346 1.000 23.21 ATOM 96 CA GLY A 23 70.440 6.507 34.447 1.000 25.79 ATOM 97 C GLY A 23 69.358 5.770 35.216 1.000 26.66 ATOM 98 O GLY A 23 68.186 5.751 34.825 1.000 23.79 ATOM 99 N LEU A 24 69.752 5.161 36.337 1.000 21.40 ATOM 100 CA LEU A 24 68.777 4.449 37.166 1.000 20.59 ATOM 101 CB LEU A 24 69.496 3.755 38.319 1.000 21.40 ATOM 102 CG LEU A 24 68.626 3.074 39.371 1.000 23.90 ATOM 103 CD1 LEU A 24 67.775 1.976 38.757 1.000 22.46 ATOM 104 CD2 LEU A 24 69.525 2.526 40.475 1.000 25.95 ATOM 105 C LEU A 24 67.690 5.366 37.705 1.000 22.12 ATOM 106 O LEU A 24 66.516 5.001 37.707 1.000 25.08 ATOM 107 N ALA A 25 68.066 6.552 37.171 1.000 23.29 ATOM 108 CA ALA A 25 67.095 7.482 38.735 1.000 21.28 ATOM 109 CB ALA A 25 67.803 8.645 39.410 1.000 21.52 ATOM 110 C ALA A 25 66.146 7.995 37.657 1.000 25.16 ATOM 111 O ALA A 25 64.967 8.241 37.885 1.000 26.05 ATOM 112 N THR A 26 66.688 8.160 36.448 1.000 25.64 ATOM 113 CA THR A 26 65.845 8.558 35.321 1.000 23.48 ATOM 114 CB THR A 26 66.719 8.816 34.085 1.000 25.74 ATOM 115 OG1 THR A 26 67.686 9.832 34.416 1.000 22.48 ATOM 116 CG2 THR A 26 65.892 9.364 32.937 1.000 17.61 ATOM 117 C THR A 26 64.794 7.490 35.055 1.000 21.52 ATOM 118 O THR A 26 63.610 7.767 34.864 1.000 26.28 ATOM 119 N ALA A 27 65.226 6.236 35.064 1.000 20.21 ATOM 120 CA ALA A 27 64.316 5.109 34.921 1.000 25.18 ATOM 121 CB ALA A 27 65.121 3.818 34.862 1.000 25.77 ATOM 122 C ALA A 27 63.300 5.079 36.056 1.000 28.07 ATOM 123 O ALA A 27 62.098 4.897 35.838 1.000 26.17 ATOM 124 N GLU A 28 63.759 5.262 37.299 1.000 25.77 ATOM 125 CA GLU A 28 62.793 5.280 38.403 1.000 26.24 ATOM 126 CB GLU A 28 63.509 5.474 39.747 1.000 26.43 ATOM 127 CG GLU A 28 64.155 4.190 40.239 1.000 29.26 ATOM 128 CD GLU A 28 65.322 4.364 41.176 1.000 35.43 ATOM 129 OE1 GLU A 28 65.845 3.327 41.641 1.000 39.79 ATOM 130 OE2 GLU A 28 65.725 5.511 41.457 1.000 40.51 ATOM 131 C GLU A 28 61.736 6.353 38.200 1.000 29.60 ATOM 132 O GLU A 28 60.527 6.105 38.265 1.000 24.84 ATOM 133 N ARG A 29 62.157 8.589 37.935 1.000 24.83 ATOM 134 CA ARG A 29 61.176 8.661 37.772 1.000 26.33 ATOM 135 CB ARG A 29 61.908 9.991 37.560 1.000 23.24 ATOM 136 CG ARG A 29 61.039 11.130 37.078 1.000 24.21 ATOM 137 CD ARG A 29 61.639 12.485 37.398 1.000 25.40 ATOM 138 NE ARG A 29 60.559 13.482 37.422 1.000 27.67 ATOM 139 CZ ARG A 29 60.014 13.892 38.559 1.000 30.21 ATOM 140 NH1 ARG A 29 59.042 14.791 38.527 1.000 31.45 ATOM 141 NH2 ARG A 29 60.441 13.409 39.718 1.000 29.38 ATOM 142 C ARG A 29 60.210 8.405 36.620 1.000 29.14 ATOM 143 O ARG A 29 58.992 8.557 36.761 1.000 31.80 ATOM 144 N LEU A 30 60.749 8.024 35.461 1.000 25.02 ATOM 145 CA LEU A 30 59.880 7.864 34.295 1.000 27.73 ATOM 146 CB LEU A 30 60.700 7.667 33.017 1.000 26.81 ATOM 147 CG LEU A 30 61.602 8.837 32.602 1.000 25.95 ATOM 148 CD1 LEU A 30 62.296 8.530 31.280 1.000 18.00 ATOM 149 CD2 LEU A 30 60.832 10.141 32.501 1.000 25.79 ATOM 150 C LEU A 30 58.910 6.705 34.504 1.000 32.32 ATOM 151 O LEU A 30 57.707 6.857 34.261 1.000 32.24 ATOM 152 N VAL A 31 59.420 5.555 34.951 1.000 26.53 ATOM 153 CA VAL A 31 58.504 4.438 35.202 1.000 30.92 ATOM 154 CB VAL A 31 59.228 3.177 35.690 1.000 33.99 ATOM 155 CG1 VAL A 31 58.227 2.141 36.183 1.000 41.79 ATOM 156 CG2 VAL A 31 60.092 2.582 34.586 1.000 28.28 ATOM 157 C VAL A 31 57.465 4.884 36.228 1.000 32.60 ATOM 158 O VAL A 31 56.271 4.603 36.133 1.000 35.28 ATOM 159 N GLY A 32 57.937 5.637 37.219 1.000 26.54 ATOM 160 CA GLY A 32 57.041 6.213 38.209 1.000 28.51 ATOM 161 C GLY A 32 56.043 7.178 37.602 1.000 35.42 ATOM 162 O GLY A 32 54.960 7.376 38.160 1.000 31.39 ATOM 163 N GLN A 33 56.387 7.791 36.470 1.000 36.54 ATOM 164 CA GLN A 33 55.470 8.735 35.835 1.000 35.97 ATOM 165 CB GLN A 33 56.251 9.946 35.304 1.000 39.48 ATOM 166 CG GLN A 33 56.931 10.759 36.395 1.000 44.03 ATOM 167 CD GLN A 33 55.975 11.701 37.105 1.000 48.53 ATOM 168 OE1 GLN A 33 55.142 12.349 36.469 1.000 57.31 ATOM 169 NE2 GLN A 33 56.073 11.773 38.426 1.000 58.52 ATOM 170 C GLN A 33 54.666 8.107 37.708 1.000 33.10 ATOM 171 O GLN A 33 54.151 8.809 33.835 1.000 32.11 ATOM 172 N GLY A 34 54.548 6.786 34.698 1.000 30.58 ATOM 173 CA GLY A 34 53.759 6.081 33.712 1.000 30.35 ATOM 174 C GLY A 34 54.465 5.672 32.444 1.000 33.61 ATOM 175 O GLY A 34 53.842 5.118 31.529 1.000 32.81 ATOM 176 N ALA A 35 55.769 5.914 32.316 1.000 29.29 ATOM 177 CA ALA A 35 56.477 5.513 31.103 1.000 24.74 ATOM 178 CB ALA A 35 57.603 6.507 30.811 1.000 25.46 ATOM 179 C ALA A 35 57.043 4.110 31.214 1.000 25.25 ATOM 180 O ALA A 35 57.104 3.509 32.287 1.000 29.96 ATOM 181 N SER A 36 57.502 3.540 30.094 1.000 27.78 ATOM 182 CA SER A 36 58.197 2.255 30.188 1.000 29.92 ATOM 183 CB SER A 36 57.665 1.248 29.173 1.000 29.14 ATOM 184 OG SER A 36 56.246 1.180 29.229 1.000 34.85 ATOM 185 C SER A 36 59.693 2.474 29.987 1.000 34.68 ATOM 186 O SER A 36 60.112 3.339 29.199 1.000 29.89 ATOM 187 N ALA A 37 60.520 1.704 30.699 1.000 69.94 ATOM 188 CA ALA A 37 61.956 1.937 30.534 1.000 29.90 ATOM 189 CB ALA A 37 62.525 2.620 31.769 1.000 27.09 ATOM 190 C ALA A 37 62.702 0.647 30.219 1.000 26.26 ATOM 191 O ALA A 37 62.390 −0.426 30.728 1.000 32.04 ATOM 192 N VAL A 38 63.695 0.788 29.354 1.000 23.68 ATOM 193 CA VAL A 38 64.637 −0.263 29.023 1.000 22.95 ATOM 194 CB VAL A 38 64.811 −0.441 27.504 1.000 25.74 ATOM 195 CG1 VAL A 38 65.856 −1.513 27.223 1.000 24.56 ATOM 196 CG2 VAL A 38 63.491 −0.774 26.830 1.000 32.06 ATOM 197 C VAL A 38 65.997 0.093 29.617 1.000 28.45 ATOM 198 O VAL A 38 66.594 1.082 29.173 1.000 26.25 ATOM 199 N LEU A 39 66.491 −0.659 30.600 1.000 27.75 ATOM 200 CA LEU A 39 67.800 −0.311 31.164 1.000 25.11 ATOM 201 CB LEU A 39 67.947 −0.783 32.608 1.000 24.71 ATOM 202 CG LEU A 39 66.802 −0.447 33.563 1.000 22.78 ATOM 203 CD1 LEU A 39 67.098 −0.949 34.969 1.000 22.70 ATOM 204 CD2 LEU A 39 66.523 1.047 33.573 1.000 21.30 ATOM 205 C LEU A 39 68.904 −0.910 30.305 1.000 25.85 ATOM 206 O LEU A 39 69.165 −2.113 30.378 1.000 29.36 ATOM 207 N LEU A 40 69.548 −0.085 29.480 1.000 24.69 ATOM 208 CA LEU A 40 70.644 −0.615 28.655 1.000 22.81 ATOM 209 CB LEU A 40 70.642 0.066 27.298 1.000 19.59 ATOM 210 CG LEU A 40 71.463 −0.528 26.158 1.000 25.17 ATOM 211 CD1 LEU A 40 70.956 −0.022 24.814 1.000 27.01 ATOM 212 CD2 LEU A 40 72.940 −0.191 26.275 1.000 26.56 ATOM 213 C LEU A 40 71.962 −0.442 29.410 1.000 26.53 ATOM 214 O LEU A 40 72.434 0.664 29.672 1.000 25.35 ATOM 215 N ASP A 41 72.575 −1.561 29.783 1.000 28.32 ATOM 216 CA ASP A 41 73.804 −1.500 30.579 1.000 27.97 ATOM 217 CB ASP A 41 73.454 −1.175 32.031 1.000 21.96 ATOM 218 CG ASP A 41 74.535 −0.431 32.778 1.000 27.64 ATOM 219 OD1 ASP A 41 75.708 −0.851 32.693 1.000 27.85 ATOM 220 OD2 ASP A 41 74.235 0.571 33.459 1.000 25.29 ATOM 221 C ASP A 41 74.559 −2.815 30.443 1.000 28.71 ATOM 222 O ASP A 41 74.000 −3.774 29.901 1.000 26.54 ATOM 223 N LEU A 42 72.795 −2.879 30.910 1.000 26.54 ATOM 224 CA LEU A 42 76.641 −4.055 30.732 1.000 28.04 ATOM 225 CB LEU A 42 78.055 −3.751 31.262 1.000 27.78 ATOM 226 CG LEU A 42 78.868 −2.727 30.459 1.000 29.86 ATOM 227 CD1 LEU A 42 80.180 −2.423 31.172 1.000 26.34 ATOM 228 CD2 LEU A 42 79.126 −3.212 29.043 1.000 18.86 ATOM 229 C LEU A 42 76.098 −5.293 31.423 1.000 26.58 ATOM 230 O LEU A 42 75.344 −5.204 32.392 1.000 23.94 ATOM 231 N PRO A 43 76.468 −6.473 30.947 1.000 30.41 ATOM 232 CD PRO A 43 77.291 −6.725 29.753 1.000 31.03 ATOM 233 CA PRO A 43 76.042 −7.716 31.593 1.000 32.05 ATOM 234 CB PRO A 43 76.767 −8.808 30.796 1.000 29.32 ATOM 235 CB PRO A 43 77.035 −8.184 29.469 1.000 32.03 ATOM 236 C PRO A 43 76.484 −7.799 33.046 1.000 33.41 ATOM 237 O PRO A 43 75.756 −8.304 33.911 1.000 37.54 ATOM 238 N ASN A 44 77.685 −7.316 33.356 1.000 31.95 ATOM 239 CA ASN A 44 78.146 −7.453 34.744 1.000 40.41 ATOM 240 CB ASN A 44 79.668 −7.347 34.827 1.000 49.11 ATOM 241 CG ASN A 44 80.196 −6.236 33.938 1.000 49.11 ATOM 242 OD1 ASN A 44 80.617 −6.491 32.805 1.000 69.12 ATOM 243 ND2 ASN A 44 80.167 −5.006 34.446 1.000 62.20 ATOM 244 C ASN A 44 77.490 −6.415 35.636 1.000 38.34 ATOM 245 O ASN A 44 77.624 −6.435 36.861 1.000 41.33 ATOM 246 N SER A 45 76.741 −5.475 35.053 1.000 35.28 ATOM 247 CA SER A 45 76.052 −4.530 35.939 1.000 32.87 ATOM 248 CB SER A 45 75.622 −3.278 35.188 1.000 31.87 ATOM 249 OG SER A 45 74.642 −3.582 34.212 1.000 29.60 ATOM 250 C SER A 45 74.863 −5.241 36.578 1.000 37.42 ATOM 251 O SER A 45 74.533 −6.370 36.209 1.000 64.40 ATOM 252 N GLY A 46 74.217 −4.587 37.537 1.000 34.25 ATOM 253 CA GLY A 46 73.055 −5.178 38.181 1.000 31.85 ATOM 254 C GLY A 46 71.759 −4.755 37.526 1.000 30.67 ATOM 255 O GLY A 46 70.729 −4.609 38.193 1.000 33.01 ATOM 256 N GLY A 47 71.756 −4.541 36.209 1.000 29.41 ATOM 257 CA GLY A 47 70.527 −4.137 35.549 1.000 30.70 ATOM 258 C GLY A 47 69.377 −5.097 35.791 1.000 33.15 ATOM 259 O GLY A 47 68.247 −4.677 36.065 1.000 31.89 ATOM 260 N GLU A 48 69.659 −6.397 35.698 1.000 32.03 ATOM 261 CA GLU A 48 68.588 −7.391 35.804 1.000 31.42 ATOM 262 CB GLU A 48 69.127 −8.815 35.682 1.000 37.80 ATOM 263 CG GLU A 48 68.132 −9.893 35.337 1.000 47.30 ATOM 264 CD GLU A 48 66.763 −9.448 34.885 1.000 58.32 ATOM 265 OE1 GLU A 48 65.804 −9.621 35.670 1.000 65.85 ATOM 266 OE2 GLU A 48 66.612 −8.930 33.758 1.000 70.00 ATOM 267 C GLU A 48 67.846 −7.239 37.118 1.000 30.92 ATOM 268 O GLU A 48 66.617 −7.218 37.178 1.000 36.04 ATOM 269 N ALA A 49 68.606 −7.117 38.205 1.000 31.19 ATOM 270 CA ALA A 49 67.948 −6.896 39.494 1.000 31.65 ATOM 271 CB ALA A 49 68.978 −7.001 40.610 1.000 31.46 ATOM 272 C ALA A 49 67.228 −5.537 39.519 1.000 30.98 ATOM 273 O ALA A 49 66.139 −5.435 40.085 1.000 27.23 ATOM 274 N GLN A 50 67.816 −4.515 38.920 1.000 29.45 ATOM 275 CA GLN A 50 67.152 −3.211 38.984 1.000 26.50 ATOM 276 CB GLN A 50 68.110 −2.104 38.549 1.000 26.43 ATOM 277 CG GLN A 50 69.247 −1.827 39.512 1.000 26.86 ATOM 278 CD GLN A 50 68.821 −1.263 40.853 1.000 31.76 ATOM 279 OE1 GLN A 50 69.636 −1.155 41.777 1.000 48.35 ATOM 280 NE2 GLN A 50 67.557 −0.892 41.009 1.000 25.67 ATOM 281 C GLN A 50 65.893 −3.202 38.123 1.000 26.83 ATOM 282 O GLN A 50 64.914 −2.541 38.469 1.000 28.11 ATOM 283 N ALA A 51 65.919 −3.926 37.003 1.000 26.24 ATOM 284 CA ALA A 51 64.730 −4.022 36.163 1.000 29.19 ATOM 285 CB ALA A 51 65.064 −4.714 34.851 1.000 29.30 ATOM 286 C ALA A 51 63.604 −4.759 36.880 1.000 31.69 ATOM 287 O ALA A 51 62.434 −4.410 36.725 1.000 29.70 ATOM 288 CB LYS A 52 63.436 −7.768 39.045 1.000 39.33 ATOM 289 C LYS A 52 62.289 −5.597 39.496 1.000 32.07 ATOM 290 O LYS A 52 61.074 −5.564 39.705 1.000 31.48 ATOM 291 N LYS A 52 63.934 −5.779 37.666 1.000 31.15 ATOM 292 CA LYS A 53 62.895 −6.487 38.421 1.000 33.63 ATOM 293 N LYS A 53 63.132 −4.849 40.206 1.000 31.94 ATOM 294 CA LYS A 53 62.646 −3.936 41.231 1.000 33.54 ATOM 295 CB LYS A 53 63.805 −3.177 41.871 1.000 35.96 ATOM 296 CG LYS A 53 64.746 −3.962 42.758 1.000 43.20 ATOM 297 CD LYS A 53 65.258 −3.055 43.877 1.000 49.44 ATOM 298 CE LYS A 53 64.198 −2.022 44.244 1.000 50.60 ATOM 299 NZ LYS A 53 64.784 −0.830 44.919 1.000 60.33 ATOM 300 C LYS A 53 61.671 −2.908 40.672 1.000 36.81 ATOM 301 O LYS A 53 60.745 −2.481 41.369 1.000 40.69 ATOM 302 N LEU A 54 61.855 −2.468 39.423 1.000 35.85 ATOM 303 CA LEU A 54 61.021 −1.353 38.960 1.000 32.59 ATOM 304 CB LEU A 54 61.779 −0.549 37.886 1.000 28.86 ATOM 305 CG LEU A 54 62.665 0.555 38.491 1.000 30.10 ATOM 306 CD1 LEU A 54 63.603 1.152 37.459 1.000 29.65 ATOM 307 CD2 LEU A 54 61.779 1.617 39.126 1.000 29.77 ATOM 308 C LEU A 54 59.660 −1.797 38.457 1.000 31.24 ATOM 309 O LEU A 54 58.766 −0.954 38.352 1.000 39.12 ATOM 310 N GLY A 55 59.484 −3.081 38.163 1.000 34.66 ATOM 311 CA GLY A 55 59.174 −3.601 37.829 1.000 29.84 ATOM 312 C GLY A 55 58.004 −4.016 36.387 1.000 30.24 ATOM 313 O GLY A 55 58.972 −4.176 35.645 1.000 27.18 ATOM 314 N ASN A 56 56.747 −4.198 35.985 1.000 32.93 ATOM 315 CA ASN A 56 56.409 −4.664 34.650 1.000 38.74 ATOM 316 CB ASN A 56 54.896 −4.906 34.554 1.000 45.27 ATOM 317 CG ASN A 56 54.472 −6.105 35.376 1.000 52.39 ATOM 318 OD1 ASN A 56 53.386 −6.091 35.948 1.000 62.55 ATOM 319 ND2 ASN A 56 55.334 −7.116 35.417 1.000 51.01 ATOM 320 C ASN A 56 56.802 −3.691 33.548 1.000 36.08 ATOM 321 O ASN A 56 56.989 −4.108 32.400 1.000 37.33 ATOM 322 N ASN A 57 56.905 −2.405 33.885 1.000 35.54 ATOM 323 CA ASN A 57 57.123 −1.426 32.816 1.000 34.82 ATOM 324 CB ASN A 57 56.314 −0.156 33.089 1.000 33.64 ATOM 325 CG ASN A 57 54.817 −0.410 33.105 1.000 38.38 ATOM 326 OD1 ASN A 57 54.099 0.174 33.917 1.000 46.58 ATOM 327 ND2 ASN A 57 54.352 −1.283 32.219 1.000 39.66 ATOM 328 C ASN A 57 58.601 −1.096 32.641 1.000 35.06 ATOM 329 O ASN A 57 58.952 −0.061 32.068 1.000 29.66 ATOM 330 N CYS A 58 59.463 −1.981 33.132 1.000 32.26 ATOM 331 CA CYS A 58 60.908 −1.788 33.018 1.000 31.63 ATOM 332 CB CYS A 58 61.453 −1.136 34.299 1.000 30.13 ATOM 333 SG CYS A 58 63.247 −0.942 34.332 1.000 30.84 ATOM 334 C CYS A 58 61.686 −3.094 32.749 1.000 28.19 ATOM 335 O CYS A 58 61.469 −4.089 33.455 1.000 31.62 ATOM 336 N VAL A 59 62.479 −3.139 31.716 1.000 29.67 ATOM 337 CA VAL A 59 63.231 −4.367 31.450 1.000 27.92 ATOM 338 CB VAL A 59 62.717 −5.090 30.193 1.000 34.40 ATOM 339 CG1 VAL A 59 61.194 −5.189 30.205 1.000 35.21 ATOM 340 CG2 VAL A 59 63.186 −4.379 28.931 1.000 33.09 ATOM 341 C VAL A 59 64.720 −4.068 31.305 1.000 30.47 ATOM 342 O VAL A 59 65.109 −2.914 31.099 1.000 30.32 ATOM 343 N PHE A 60 65.540 −5.106 31.414 1.000 28.13 ATOM 344 CA PHE A 60 66.984 −4.984 31.257 1.000 27.53 ATOM 345 CB PHE A 60 67.699 −5.719 32.386 1.000 26.77 ATOM 346 CG PHE A 60 69.197 −5.879 32.228 1.000 29.40 ATOM 347 CD1 PHE A 60 70.027 −4.793 32.017 1.000 30.82 ATOM 348 CD2 PHE A 60 69.775 −7.134 32.295 1.000 30.46 ATOM 349 CE1 PHE A 60 71.391 −4.955 31.880 1.000 28.83 ATOM 350 CE2 PHE A 60 71.144 −7.301 32.157 1.000 28.61 ATOM 351 CZ PHE A 60 71.963 −6.211 31.948 1.000 26.40 ATOM 352 C PHE A 60 67.430 −5.520 29.900 1.000 31.03 ATOM 353 O PHE A 60 67.112 −6.641 29.507 1.000 28.03 ATOM 354 N ALA A 61 68.183 −4.708 29.165 1.000 29.19 ATOM 355 CA ALA A 61 68.787 −5.142 27.909 1.000 25.43 ATOM 356 CB ALA A 61 68.346 −4.273 26.748 1.000 28.07 ATOM 357 C ALA A 61 70.306 −5.101 28.044 1.000 28.34 ATOM 358 O ALA A 61 70.876 −4.007 28.104 1.000 32.03 ATOM 359 N PRO A 62 70.940 −6.263 28.112 1.000 30.23 ATOM 360 CD PRO A 62 70.344 −7.605 28.031 1.000 27.38 ATOM 361 CA PRO A 62 72.397 −6.292 28.287 1.000 29.81 ATOM 362 CB PRO A 62 72.692 −7.775 28.525 1.000 28.87 ATOM 363 CG PRO A 62 71.543 −8.503 27.920 1.000 28.71 ATOM 364 C PRO A 62 73.114 −5.792 27.042 1.000 29.91 ATOM 365 O PRO A 62 72.857 −6.253 25.926 1.000 31.43 ATOM 366 N ALA A 63 74.026 −4.836 27.200 1.000 23.31 ATOM 367 CA ALA A 63 74.725 −4.334 26.017 1.000 27.56 ATOM 368 CB ALA A 63 73.754 −3.643 25.064 1.000 24.43 ATOM 369 C ALA A 63 75.845 −3.363 26.369 1.000 23.71 ATOM 370 O ALA A 63 75.730 −2.283 27.305 1.000 27.32 ATOM 371 N ASP A 64 76.910 −3.416 25.594 1.000 24.90 ATOM 372 CA ASP A 64 78.039 −2.504 25.601 1.000 27.05 ATOM 373 CB ASP A 64 79.335 −3.280 25.359 1.000 24.11 ATOM 374 CG ASP A 64 80.575 −2.425 25.459 1.000 27.69 ATOM 375 OD1 ASP A 64 81.672 −2.969 25.700 1.000 32.95 ATOM 376 OD2 ASP A 64 80.481 −1.188 25.299 1.000 29.28 ATOM 377 C ASP A 64 77.816 −1.455 24.513 1.000 26.63 ATOM 378 O ASP A 64 77.662 −1.864 23.353 1.000 23.13 ATOM 379 N VAL A 65 77.773 −0.175 24.870 1.000 28.62 ATOM 380 CA VAL A 65 77.445 0.878 23.913 1.000 25.22 ATOM 381 CB VAL A 65 77.169 2.252 24.562 1.000 22.72 ATOM 382 CG1 VAL A 65 75.934 2.199 25.445 1.000 19.07 ATOM 383 CG2 VAL A 65 78.382 2.737 25.354 1.000 22.83 ATOM 384 C VAL A 65 78.545 1.085 22.882 1.000 22.70 ATOM 385 O VAL A 65 78.316 1.783 21.891 1.000 26.47 ATOM 386 N THR A 66 79.731 0.513 23.074 1.000 21.37 ATOM 387 CA THR A 66 80.742 0.660 22.027 1.000 23.63 ATOM 388 CB THR A 66 82.175 0.536 22.567 1.000 26.03 ATOM 389 OG1 THR A 66 82.330 −0.756 23.182 1.000 28.93 ATOM 390 CG1 THR A 66 82.437 1.562 23.658 1.000 26.52 ATOM 391 C THR A 66 80.567 −0.391 20.934 1.000 27.05 ATOM 392 O THR A 66 81.322 −0.413 19.966 1.000 27.67 ATOM 393 N SER A 67 79.588 −1.273 21.068 1.000 28.37 ATOM 394 CA SER A 67 79.390 −2.367 20.128 1.000 27.49 ATOM 395 CB SER A 67 79.300 −3.686 20.904 1.000 23.12 ATOM 396 OG SER A 67 78.456 −4.607 20.235 1.000 28.63 ATOM 397 C SER A 67 78.143 −2.202 19.266 1.000 27.54 ATOM 398 O SER A 67 77.027 −2.082 19.789 1.000 28.72 ATOM 399 N GLU A 68 78.325 −2.214 17.942 1.000 27.74 ATOM 400 CA GLU A 68 77.192 −2.102 17.028 1.000 29.78 ATOM 401 CB GLU A 68 77.652 −2.183 15.560 1.000 30.35 ATOM 402 CG GLU A 68 76.501 −1.980 14.588 1.000 33.75 ATOM 403 CD GLU A 68 76.933 −1.791 13.150 1.000 37.21 ATOM 404 OE1 GLU A 68 77.152 −0.638 12.731 1.000 36.37 ATOM 405 OE2 GLU A 68 77.055 −2.805 12.432 1.000 44.18 ATOM 406 C GLU A 68 76.153 −3.186 17.271 1.000 27.83 ATOM 407 O GLU A 68 74.964 −2.915 17.443 1.000 26.11 ATOM 408 CB LYS A 69 76.372 −6.876 17.184 1.000 34.15 ATOM 409 C LYS A 69 74.896 −5.512 18.692 1.000 29.20 ATOM 410 O LYS A 69 73.680 −5.745 18.740 1.000 28.05 ATOM 411 N LYS A 69 76.601 −4.442 17.264 1.000 24.54 ATOM 412 CA LYS A 69 75.653 −5.551 17.369 1.000 27.59 ATOM 413 N ASP A 70 75.589 −5.223 19.791 1.000 26.28 ATOM 414 CA ASP A 70 74.905 −5.189 21.085 1.000 28.59 ATOM 415 CB ASP A 70 75.891 −4.867 22.211 1.000 30.01 ATOM 416 CG ASP A 70 76.714 −6.064 22.626 1.000 30.41 ATOM 417 OD1 ASP A 70 76.556 −7.136 22.014 1.000 32.46 ATOM 418 OD2 ASP A 70 77.520 −5.919 23.568 1.000 31.67 ATOM 419 C ASP A 70 73.785 −4.161 21.118 1.000 25.48 ATOM 420 O ASP A 70 72.673 −4.412 21.582 1.000 28.32 ATOM 421 N VAL A 71 74.102 −2.962 20.614 1.000 27.50 ATOM 422 CA VAL A 71 73.073 −1.917 20.648 1.000 25.54 ATOM 423 CB VAL A 71 73.667 −0.550 20.280 1.000 25.70 ATOM 424 CG1 VAL A 71 72.592 0.519 20.166 1.000 23.17 ATOM 425 CG2 VAL A 71 74.711 −0.143 21.315 1.000 27.59 ATOM 426 C VAL A 71 71.932 −2.316 19.723 1.000 25.05 ATOM 427 O VAL A 71 70.750 −2.147 20.019 1.000 26.83 ATOM 428 N GLN A 72 72.293 −2.883 18.574 1.000 24.81 ATOM 429 CA GLN A 72 71.261 −3.431 17.693 1.000 29.31 ATOM 430 CB GLN A 72 71.918 −4.055 16.465 1.000 28.74 ATOM 431 CG GLN A 72 72.472 −3.031 15.482 1.000 30.16 ATOM 432 CD GLN A 72 73.120 −3.697 14.283 1.000 36.36 ATOM 433 OE1 GLN A 72 73.821 −4.699 14.442 1.000 43.12 ATOM 434 NE2 GLN A 72 72.895 −3.153 13.093 1.000 40.74 ATOM 435 C GLN A 72 70.418 −4.454 18.439 1.000 26.93 ATOM 436 O GLN A 72 69.191 −4.448 18.377 1.000 30.79 ATOM 437 N THR A 73 71.069 −5.359 19.173 1.000 26.15 ATOM 438 CA THR A 73 70.306 −6.375 19.901 1.000 30.40 ATOM 439 CB THR A 73 71.227 −7.417 20.561 1.000 37.27 ATOM 440 OG1 THR A 73 72.116 −7.998 19.599 1.000 36.22 ATOM 441 OG2 THR A 73 70.393 −8.571 21.103 1.000 35.78 ATOM 442 C THR A 73 69.410 −5.755 20.963 1.000 32.05 ATOM 443 O THR A 73 68.253 −6.130 21.181 1.000 36.06 ATOM 444 N ALA A 74 69.935 −4.759 21.681 1.000 27.56 ATOM 445 CA ALA A 74 69.125 −4.130 22.719 1.000 23.23 ATOM 446 CB ALA A 74 70.014 −3.240 23.579 1.000 27.20 ATOM 447 C ALA A 74 67.975 −3.327 22.143 1.000 27.14 ATOM 448 O ALA A 74 66.920 −3.170 22.769 1.000 32.32 ATOM 449 N LEU A 75 68.124 −2.755 20.943 1.000 27.14 ATOM 450 CA LEU A 75 67.004 −1.940 20.453 1.000 27.09 ATOM 451 CB LEU A 75 67.496 −1.012 19.342 1.000 27.14 ATOM 452 CG LEU A 75 68.362 0.157 19.824 1.000 26.32 ATOM 453 CD1 LEU A 75 68.833 1.022 18.667 1.000 27.27 ATOM 454 CD2 LEU A 75 67.602 1.004 20.836 1.000 23.37 ATOM 455 C LEU A 75 65.856 −2.839 20.007 1.000 26.19 ATOM 456 O LEU A 75 64.673 −2.555 20.198 1.000 26.12 ATOM 457 N ALA A 76 66.226 −3.955 19.394 1.000 28.48 ATOM 458 CA ALA A 76 65.291 −4.987 18.974 1.000 32.72 ATOM 459 CB ALA A 76 66.033 −6.067 18.194 1.000 30.42 ATOM 460 C ALA A 76 64.584 −5.562 20.191 1.000 36.42 ATOM 461 O ALA A 76 63.386 −5.845 20.160 1.000 35.82 ATOM 462 N LEU A 77 65.323 −5.733 21.287 1.000 34.58 ATOM 463 CA LEU A 77 64.675 −6.174 22.526 1.000 30.05 ATOM 464 CB LEU A 77 65.706 −6.374 23.623 1.000 32.29 ATOM 465 CG LEU A 77 65.256 −6.961 24.965 1.000 35.67 ATOM 466 CD1 LEU A 77 66.370 −7.768 25.618 1.000 39.63 ATOM 467 CD2 LEU A 77 64.799 −5.868 25.922 1.000 31.59 ATOM 468 C LEU A 77 63.621 −5.149 22.927 1.000 32.17 ATOM 469 O LEU A 77 62.499 −5.499 23.299 1.000 35.79 ATOM 470 N ALA A 78 64.007 −3.875 22.853 1.000 29.62 ATOM 471 CA ALA A 78 63.101 −2.822 23.307 1.000 32.17 ATOM 472 CB ALA A 78 63.822 −1.483 23.336 1.000 32.12 ATOM 473 C ALA A 78 61.849 −2.748 22.447 1.000 30.46 ATOM 474 O ALA A 78 60.731 −2.575 22.946 1.000 30.23 ATOM 475 N LYS A 79 62.013 −2.876 21.133 1.000 33.18 ATOM 476 CA LYS A 79 60.833 −2.810 20.266 1.000 36.74 ATOM 477 CB LYS A 79 61.245 −2.779 18.804 1.000 33.27 ATOM 478 C LYS A 79 59.908 −3.987 20.553 1.000 38.51 ATOM 479 O LYS A 79 58.725 −3.833 20.865 1.000 37.04 ATOM 480 N GLY A 80 60.457 −5.196 20.455 1.000 38.59 ATOM 481 CA GLY A 80 59.683 −6.401 20.700 1.000 40.57 ATOM 482 C GLY A 80 58.971 −6.362 22.035 1.000 42.68 ATOM 483 O GLY A 80 57.842 −6.835 22.193 1.000 43.09 ATOM 484 N LYS A 81 59.614 −5.779 23.052 1.000 37.05 ATOM 485 CA LYS A 81 58.951 −5.799 24.356 1.000 34.36 ATOM 486 CB LYS A 81 59.988 −5.738 25.482 1.000 39.39 ATOM 487 CG LYS A 81 59.370 −5.571 26.863 1.000 47.54 ATOM 488 CD LYS A 81 58.961 −6.918 27.443 1.000 53.39 ATOM 489 CE LYS A 81 57.911 −6.741 28.529 1.000 57.33 ATOM 490 NZ LYS A 81 57.931 −7.873 29.500 1.000 62.03 ATOM 491 C LYS A 81 57.947 −4.670 24.506 1.000 35.60 ATOM 492 O LYS A 81 56.870 −4.863 25.069 1.000 33.46 ATOM 493 N PHE A 82 58.271 −3.472 24.015 1.000 32.89 ATOM 494 CA PHE A 82 57.382 −2.357 24.335 1.000 31.56 ATOM 495 CB PHE A 82 58.129 −1.303 25.161 1.000 34.84 ATOM 496 CG PHE A 82 58.418 −1.752 26.585 1.000 33.59 ATOM 497 CD1 PHE A 82 57.406 −2.221 27.406 1.000 31.18 ATOM 498 CD2 PHE A 82 59.712 −1.693 27.081 1.000 30.71 ATOM 499 CE1 PHE A 82 57.690 −2.623 28.698 1.000 34.47 ATOM 500 CE2 PHE A 82 60.002 −2.097 28.371 1.000 30.31 ATOM 501 CZ PHE A 82 58.987 −2.563 29.185 1.000 33.43 ATOM 502 C PHE A 82 56.760 −1.710 23.107 1.000 33.34 ATOM 503 O PHE A 82 55.969 −0.783 23.304 1.000 35.24 ATOM 504 N GLY A 83 57.098 −2.188 21.916 1.000 35.59 ATOM 505 CA GLY A 83 56.424 −1.757 20.707 1.000 37.30 ATOM 506 C GLY A 83 57.132 −0.690 19.906 1.000 40.28 ATOM 507 O GLY A 83 57.141 −0.747 18.668 1.000 38.84 ATOM 508 N ARG A 84 57.724 0.292 20.573 1.000 36.22 ATOM 509 CA ARG A 84 58.472 1.354 19.917 1.000 33.53 ATOM 510 CB ARG A 84 57.523 2.420 19.371 1.000 28.51 ATOM 511 CG ARG A 84 56.638 3.117 20.390 1.000 34.98 ATOM 512 CD ARG A 84 56.394 4.574 20.015 1.000 44.46 ATOM 513 NE ARG A 84 55.513 4.720 18.871 1.000 52.06 ATOM 514 CZ ARG A 84 55.176 5.811 18.208 1.000 56.54 ATOM 515 NH1 ARG A 84 54.338 5.706 17.176 1.000 63.82 ATOM 516 NH2 ARG A 84 55.641 7.015 18.527 1.000 33.88 ATOM 517 C ARG A 84 59.483 7.015 20.882 1.000 34.32 ATOM 518 O ARG A 84 59.515 1.588 22.052 1.000 37.33 ATOM 519 N VAL A 85 60.264 2.925 20.388 1.000 28.25 ATOM 520 CA VAL A 85 61.157 3.768 21.179 1.000 26.10 ATOM 521 CB VAL A 85 62.635 3.482 20.862 1.000 28.04 ATOM 522 CG1 VAL A 85 63.551 4.419 21.629 1.000 28.94 ATOM 523 CG2 VAL A 85 62.983 2.037 21.191 1.000 24.86 ATOM 524 C VAL A 85 60.849 5.242 20.922 1.000 26.87 ATOM 525 O VAL A 85 60.849 5.696 19.775 1.000 28.91 ATOM 526 N ASP A 86 60.565 5.994 21.974 1.000 27.02 ATOM 527 CA ASP A 86 60.191 7.394 21.880 1.000 25.13 ATOM 528 CB ASP A 86 58.914 7.687 22.679 1.000 26.20 ATOM 529 CG ASP A 86 57.755 6.817 22.227 1.000 32.00 ATOM 530 OD1 ASP A 86 57.283 5.983 23.028 1.000 31.29 ATOM 531 OD2 ASP A 86 57.330 6.991 21.070 1.000 32.98 ATOM 532 C ASP A 86 61.287 8.298 22.434 1.000 27.98 ATOM 533 O ASP A 86 61.426 9.448 22.029 1.000 23.19 ATOM 534 N VAL A 87 62.044 7.759 23.386 1.000 21.53 ATOM 535 CA VAL A 87 63.071 8.542 24.056 1.000 20.22 ATOM 536 CB VAL A 87 62.603 8.986 25.458 1.000 26.46 ATOM 537 CG1 VAL A 87 63.720 9.700 26.207 1.000 24.62 ATOM 538 CG2 VAL A 87 61.388 9.895 25.352 1.000 25.17 ATOM 539 C VAL A 87 64.351 7.740 24.198 1.000 23.75 ATOM 540 O VAL A 87 64.311 6.537 24.472 1.000 26.72 ATOM 541 N ALA A 88 65.488 8.400 24.013 1.000 22.89 ATOM 542 CA ALA A 88 66.760 7.766 24.350 1.000 21.75 ATOM 543 CB ALA A 88 67.562 7.361 23.128 1.000 20.27 ATOM 544 C ALA A 88 67.554 8.732 25.234 1.000 24.86 ATOM 545 O ALA A 88 67.614 9.931 24.941 1.000 25.52 ATOM 546 N VAL A 89 68.133 8.190 26.290 1.000 22.71 ATOM 547 CA VAL A 89 68.941 8.943 27.242 1.000 21.03 ATOM 548 CB VAL A 89 68.273 9.059 28.619 1.000 26.69 ATOM 549 CG1 VAL A 89 69.077 9.959 29.552 1.000 22.65 ATOM 550 CG2 VAL A 89 66.854 9.602 28.502 1.000 19.47 ATOM 551 C VAL A 89 70.291 8.249 27.383 1.000 20.81 ATOM 552 O VAL A 89 70.347 7.096 27.818 1.000 22.03 ATOM 553 N ASN A 90 71.367 8.939 27.005 1.000 19.58 ATOM 554 CA ASN A 90 72.695 8.336 27.105 1.000 21.95 ATOM 555 CB ASN A 90 73.590 8.778 25.940 1.000 20.86 ATOM 556 CG ASN A 90 73.116 8.208 24.611 1.000 24.64 ATOM 557 OD1 ASN A 90 72.514 8.903 23.785 1.000 25.87 ATOM 558 ND2 ASN A 90 73.396 6.930 24.405 1.000 19.47 ATOM 559 C ASN A 90 73.346 8.680 28.440 1.000 25.33 ATOM 560 O ASN A 90 73.842 9.790 28.609 1.000 24.77 ATOM 561 N CYS A 91 73.353 7.734 29.377 1.000 22.76 ATOM 562 CA CYS A 91 74.035 7.962 30.646 1.000 24.30 ATOM 563 CB CYS A 91 73.078 7.785 31.830 1.000 21.56 ATOM 564 SG CYS A 91 71.780 9.046 31.900 1.000 26.30 ATOM 565 C CYS A 91 75.244 7.045 30.818 1.000 26.70 ATOM 566 O CYS A 91 76.075 7.325 31.693 1.000 23.50 ATOM 567 N ALA A 92 75.370 5.987 30.014 1.000 24.53 ATOM 568 CA ALA A 92 76.584 5.164 30.095 1.000 25.46 ATOM 569 CB ALA A 92 76.617 4.053 29.056 1.000 17.19 ATOM 570 C ALA A 92 77.828 6.029 29.938 1.000 29.08 ATOM 571 O ALA A 92 77.960 6.832 29.012 1.000 21.74 ATOM 572 N GLY A 93 78.761 5.870 30.863 1.000 26.43 ATOM 573 CA GLY A 93 79.968 6.688 30.863 1.000 21.76 ATOM 574 C GLY A 93 80.973 6.213 31.898 1.000 26.37 ATOM 575 O GLY A 93 80.618 5.566 32.884 1.000 21.56 ATOM 576 N ILE A 94 82.241 6.549 31.675 1.000 22.95 ATOM 577 CA ILE A 94 83.284 6.187 32.626 1.000 23.39 ATOM 578 CB ILE A 94 84.202 5.061 32.107 1.000 23.77 ATOM 579 CG2 ILE A 94 83.443 3.739 32.043 1.000 23.99 ATOM 580 CG1 ILE A 94 84.872 5.403 30.774 1.000 26.25 ATOM 581 CD1 ILE A 94 85.890 4.373 30.312 1.000 27.52 ATOM 582 C ILE A 94 84.136 7.411 32.952 1.000 25.18 ATOM 583 O ILE A 94 84.147 8.392 32.212 1.000 20.18 ATOM 584 N ALA A 95 84.841 7.327 34.071 1.000 30.99 ATOM 585 CA ALA A 95 85.701 8.409 34.529 1.000 31.12 ATOM 586 CB ALA A 95 85.203 8.956 35.861 1.000 25.55 ATOM 587 C ALA A 95 87.133 7.924 34.689 1.000 30.69 ATOM 588 O ALA A 95 87.340 6.756 35.011 1.000 26.55 ATOM 589 N VAL A 96 88.101 8.803 34.473 1.000 26.73 ATOM 590 CA VAL A 96 89.465 8.504 37.874 1.000 25.75 ATOM 591 CB VAL A 96 90.383 7.900 33.795 1.000 35.08 ATOM 592 CG1 VAL A 96 89.750 6.702 33.103 1.000 52.12 ATOM 593 CG2 VAL A 96 90.760 8.960 32.768 1.000 41.24 ATOM 594 C VAL A 96 90.096 9.811 35.353 1.000 24.96 ATOM 595 O VAL A 96 89.705 10.888 34.903 1.000 24.58 ATOM 596 N ALA A 97 91.063 9.688 36.254 1.000 22.38 ATOM 597 CA ALA A 97 91.802 10.883 36.648 1.000 21.56 ATOM 598 CB ALA A 97 91.603 11.239 38.105 1.000 29.25 ATOM 599 C ALA A 97 93.265 10.618 36.313 1.000 25.19 ATOM 600 O ALA A 97 93.879 9.717 36.875 1.000 28.39 ATOM 601 N SER A 98 93.804 11.403 35.382 1.000 21.29 ATOM 602 CA SER A 98 95.185 11.135 34.382 1.000 25.00 ATOM 603 CB SER A 98 95.202 9.932 34.031 1.000 24.99 ATOM 604 OG SER A 98 96.526 9.479 33.788 1.000 24.22 ATOM 605 C SER A 98 95.751 12.391 34.346 1.000 26.54 ATOM 606 O SER A 98 95.142 12.938 34.847 1.000 22.14 ATOM 607 N LYS A 99 96.886 12.866 34.841 1.000 20.88 ATOM 608 CA LYS A 99 97.482 14.073 34.285 1.000 25.15 ATOM 609 CB LYS A 99 98.556 14.615 35.230 1.000 24.83 ATOM 610 CG LYS A 99 97.977 15.198 36.515 1.000 25.85 ATOM 611 CD LYS A 99 99.074 15.324 37.563 1.000 31.66 ATOM 612 CE LYS A 99 98.556 15.983 38.833 1.000 36.77 ATOM 613 NZ LYS A 99 99.590 16.860 39.449 1.000 50.56 ATOM 614 C LYS A 99 98.080 13.823 32.905 1.000 26.15 ATOM 615 O LYS A 99 98.577 12.729 32.630 1.000 22.84 ATOM 616 N THR A 100 98.038 14.837 32.044 1.000 20.67 ATOM 617 CA THR A 100 98.657 14.728 30.723 1.000 18.37 ATOM 618 CB THR A 100 98.611 16.080 29.989 1.000 22.10 ATOM 619 OG1 THR A 100 97.253 16.349 29.621 1.000 23.52 ATOM 620 CG2 THR A 100 99.413 16.049 28.694 1.000 21.67 ATOM 621 C THR A 100 100.108 14.269 30.845 1.000 22.79 ATOM 622 O THR A 100 100.536 13.330 30.171 1.000 21.78 ATOM 623 N TYR A 101 100.821 14.958 31.731 1.000 22.60 ATOM 624 CA TYR A 101 102.201 14.670 32.073 1.000 24.11 ATOM 625 CB TYR A 101 103.177 15.281 31.065 1.000 21.94 ATOM 626 CG TYR A 101 104.619 14.943 31.362 1.000 26.06 ATOM 627 CD1 TYR A 101 105.517 15.952 31.675 1.000 27.69 ATOM 628 CE1 TYR A 101 106.835 15.651 31.950 1.000 30.87 ATOM 629 CD2 TYR A 101 105.074 13.633 31.332 1.000 28.68 ATOM 630 CE2 TYR A 101 106.393 13.319 31.602 1.000 33.41 ATOM 631 CZ TYR A 101 107.265 14.338 31.912 1.000 32.89 ATOM 632 OH TYR A 101 108.590 14.059 32.183 1.000 29.23 ATOM 633 C TYR A 101 102.517 15.222 33.462 1.000 25.97 ATOM 634 O TYR A 101 102.057 16.312 33.799 1.000 30.11 ATOM 635 N ASN A 102 103.280 14.468 34.240 1.000 27.66 ATOM 636 CA ASN A 102 103.722 14.888 35.565 1.000 27.66 ATOM 637 CB ASN A 102 103.050 14.019 36.632 1.000 31.17 ATOM 638 CG ASN A 102 103.342 14.473 38.047 1.000 34.75 ATOM 639 OD1 ASN A 102 104.386 15.056 38.326 1.000 35.20 ATOM 640 ND2 ASN A 102 102.405 14.196 38.944 1.000 24.47 ATOM 641 C ASN A 102 105.239 14.800 35.674 1.000 24.25 ATOM 642 O ASN A 102 105.793 13.706 35.784 1.000 27.18 ATOM 643 N LEU A 103 105.917 15.938 35.639 1.000 27.28 ATOM 644 CA LEU A 103 107.377 15.978 35.641 1.000 30.32 ATOM 645 CB LEU A 103 107.862 17.419 35.527 1.000 29.30 ATOM 646 CG LEU A 103 109.359 17.699 35.508 1.000 31.61 ATOM 647 CD1 LEU A 103 110.065 16.887 34.426 1.000 34.65 ATOM 648 CD2 LEU A 103 109.639 19.177 35.284 1.000 27.84 ATOM 649 C LEU A 103 107.952 15.312 36.888 1.000 36.01 ATOM 650 O LEU A 103 108.817 14.448 36.800 1.000 38.35 ATOM 651 N LYS A 104 107.451 15.715 38.052 1.000 40.99 ATOM 652 CA LYS A 104 107.983 15.240 39.324 1.000 42.00 ATOM 653 CB LYS A 104 107.336 15.999 40.472 1.000 49.59 ATOM 654 C LYS A 104 107.803 13.738 39.480 1.000 38.56 ATOM 655 O LYS A 104 108.705 13.052 39.970 1.000 44.22 ATOM 656 N LYS A 105 106.657 13.212 39.067 1.000 33.35 ATOM 657 CA LYS A 105 106.386 11.785 39.147 1.000 33.59 ATOM 658 CB LYS A 105 104.884 11.507 39.226 1.000 42.15 ATOM 659 CG LYS A 105 104.271 11.477 40.612 1.000 51.74 ATOM 660 CD LYS A 105 103.136 10.461 40.692 1.000 61.56 ATOM 661 CE LYS A 105 103.327 9.347 39.675 1.000 67.86 ATOM 662 NZ LYS A 105 103.163 7.990 40.272 1.000 70.57 ATOM 663 C LYS A 105 106.933 11.030 37.938 1.000 31.13 ATOM 664 O LYS A 105 106.964 9.801 37.943 1.000 31.14 ATOM 665 N GLY A 106 107.340 11.761 36.902 1.000 26.45 ATOM 666 CA GLY A 106 107.796 11.094 35.685 1.000 24.64 ATOM 667 C GLY A 106 106.701 10.239 35.083 1.000 27.43 ATOM 668 O GLY A 106 106.886 9.081 34.715 1.000 32.86 ATOM 669 N GLN A 107 105.502 10.813 34.985 1.000 31.11 ATOM 670 CA GLN A 107 104.374 10.038 34.477 1.000 31.27 ATOM 671 CB GLN A 107 103.362 9.742 35.574 1.000 28.80 ATOM 672 C GLN A 107 103.696 10.751 33.303 1.000 28.71 ATOM 673 O GLN A 107 103.435 11.948 33.346 1.000 24.27 ATOM 674 N THR A 108 103.430 9.961 32.274 1.000 27.64 ATOM 675 CA THR A 108 102.755 10.383 31.062 1.000 38.26 ATOM 676 CB THR A 108 103.610 10.129 29.808 1.000 27.09 ATOM 677 OG1 THR A 108 104.883 10.783 29.912 1.000 25.29 ATOM 678 CG2 THR A 108 102.922 10.733 28.587 1.000 25.91 ATOM 679 C THR A 108 101.428 9.637 30.923 1.000 24.77 ATOM 680 O THR A 108 101.378 8.417 31.067 1.000 23.98 ATOM 681 N HIS A 109 100.355 10.364 30.653 1.000 24.32 ATOM 682 CA HIS A 109 99.051 9.760 30.368 1.000 22.88 ATOM 683 CB HIS A 109 98.089 10.835 29.870 1.000 23.80 ATOM 684 CG HIS A 109 96.630 10.563 30.566 1.000 21.82 ATOM 685 CD2 HIS A 109 95.644 11.296 30.566 1.000 22.92 ATOM 686 ND1 HIS A 109 96.003 9.467 29.439 1.000 21.44 ATOM 687 CE1 HIS A 109 94.699 9.521 29.691 1.000 21.06 ATOM 688 NE2 HIS A 109 94.463 10.622 30.380 1.000 21.74 ATOM 689 C HIS A 109 99.205 8.654 29.341 1.000 21.10 ATOM 690 O HIS A 109 99.885 8.840 28.325 1.000 25.00 ATOM 691 N THR A 110 98.632 7.478 29.588 1.000 20.94 ATOM 692 CA THR A 110 98.750 6.454 28.546 1.000 21.31 ATOM 693 CB THR A 110 98.515 5.040 29.088 1.000 24.24 ATOM 694 OG1 THR A 110 97.114 4.885 29.372 1.000 24.99 ATOM 695 CG2 THR A 110 99.305 4.818 30.376 1.000 20.99 ATOM 696 C THR A 110 97.739 6.708 27.427 1.000 24.56 ATOM 697 O THR A 110 96.963 7.326 27.615 1.000 27.87 ATOM 698 N LEU A 111 98.072 6.217 26.237 1.000 26.90 ATOM 699 CA LEU A 111 97.172 6.378 25.099 1.000 23.81 ATOM 700 CB LEU A 111 97.883 5.931 23.820 1.000 24.39 ATOM 701 CG LEU A 111 97.223 6.387 22.516 1.000 26.14 ATOM 702 CD1 LEU A 111 97.221 7.908 22.457 1.000 23.83 ATOM 703 CD2 LEU A 111 97.923 5.788 21.308 1.000 26.57 ATOM 704 C LEU A 111 95.900 5.582 25.310 1.000 25.30 ATOM 705 O LEU A 111 94.786 5.995 24.987 1.000 26.74 ATOM 706 N GLU A 112 96.019 4.371 25.856 1.000 25.49 ATOM 707 CA GLU A 112 94.818 3.548 25.972 1.000 31.39 ATOM 708 CB GLU A 112 95.191 2.092 26.246 1.000 42.44 ATOM 709 CG GLU A 112 95.339 1.235 25.003 1.000 59.05 ATOM 710 CD GLU A 112 94.763 1.797 25.003 1.000 63.34 ATOM 711 OE1 GLU A 112 93.684 1.315 23.296 1.000 56.32 ATOM 712 OE2 GLU A 112 95.377 2.706 23.110 1.000 40.30 ATOM 713 C GLU A 112 93.874 4.076 27.044 1.000 29.79 ATOM 714 O GLU A 112 92.670 3.798 26.999 1.000 25.74 ATOM 715 N ASP A 113 94.368 4.833 28.020 1.000 27.16 ATOM 716 CA ASP A 113 93.433 5.446 28.969 1.000 24.71 ATOM 717 CB ASP A 113 94.133 6.035 30.187 1.000 29.48 ATOM 718 CG ASP A 113 94.281 5.075 31.345 1.000 29.48 ATOM 719 OD1 ASP A 113 93.602 4.030 31.393 1.000 29.16 ATOM 720 OD2 ASP A 113 95.103 5.363 32.235 1.000 28.92 ATOM 721 C ASP A 113 92.648 6.540 28.253 1.000 23.27 ATOM 722 O ASP A 113 91.454 6.730 28.487 1.000 26.21 ATOM 723 N PHE A 114 93.313 7.279 27.365 1.000 21.26 ATOM 724 CA PHE A 114 92.614 8.328 26.610 1.000 21.70 ATOM 725 CB PHE A 114 93.609 9.168 25.808 1.000 21.14 ATOM 726 CG PHE A 114 93.010 10.429 25.212 1.000 22.14 ATOM 727 CD1 PHE A 114 92.544 10.432 23.907 1.000 23.21 ATOM 728 CD2 PHE A 114 92.918 11.590 25.965 1.000 19.80 ATOM 729 CE1 PHE A 114 91.993 11.579 23.354 1.000 21.77 ATOM 730 CE2 PHE A 114 92.375 12.736 25.417 1.000 22.25 ATOM 731 CZ PHE A 114 91.910 12.732 24.117 1.000 18.82 ATOM 732 C PHE A 114 91.582 7.719 25.669 1.000 21.96 ATOM 733 O PHE A 114 90.462 8.204 25.526 1.000 23.38 ATOM 734 N GLN A 115 91.989 6.632 25.021 1.000 23.07 ATOM 735 CA GLN A 115 91.174 5.965 24.017 1.000 25.81 ATOM 736 CB GLN A 115 92.006 4.911 23.278 1.000 26.74 ATOM 737 CG GLN A 115 91.332 4.324 22.045 1.000 30.43 ATOM 738 CD GLN A 115 91.298 5.316 20.896 1.000 32.36 ATOM 739 OE1 GLN A 115 91.328 5.858 20.509 1.000 34.25 ATOM 740 NE2 GLN A 115 90.114 5.565 20.352 1.000 30.37 ATOM 741 C GLN A 115 89.948 5.307 24.629 1.000 24.71 ATOM 742 O GLN A 115 88.834 5.443 24.119 1.000 27.44 ATOM 743 N ARG A 116 90.149 4.577 25.726 1.000 20.08 ATOM 744 CA ARG A 116 89.030 3.888 26.368 1.000 23.81 ATOM 745 CB ARG A 116 89.519 3.077 27.562 1.000 25.84 ATOM 746 C ARG A 116 87.944 4.868 26.808 1.000 21.73 ATOM 747 O ARG A 116 86.752 4.589 26.705 1.000 22.10 ATOM 748 N VAL A 117 88.376 6.027 27.297 1.000 22.33 ATOM 749 CA VAL A 117 87.449 7.054 27.770 1.000 21.83 ATOM 750 CB VAL A 117 88.220 8.132 28.550 1.000 21.56 ATOM 751 CG1 VAL A 117 87.409 9.401 28.744 1.000 19.07 ATOM 752 CG2 VAL A 117 88.648 7.572 29.907 1.000 26.74 ATOM 753 C VAL A 117 86.673 7.663 26.612 1.000 22.89 ATOM 754 O VAL A 117 85.461 7.877 26.721 1.000 25.91 ATOM 755 N LEU A 118 87.377 7.927 25.516 1.000 19.69 ATOM 756 CA LEU A 118 86.764 8.413 24.290 1.000 22.74 ATOM 757 CB LEU A 118 87.803 8.612 23.187 1.000 24.33 ATOM 758 CG LEU A 118 88.570 9.921 23.065 1.000 36.03 ATOM 759 CD1 LEU A 118 89.032 10.111 23.527 1.000 33.40 ATOM 760 CD2 LEU A 118 87.757 11.119 23.527 1.000 37.38 ATOM 761 C LEU A 118 85.746 7.406 23.760 1.000 22.78 ATOM 762 O LEU A 118 84.604 7.710 23.436 1.000 24.98 ATOM 763 N ASP A 119 86.218 6.164 23.658 1.000 22.45 ATOM 764 CA ASP A 119 85.406 5.118 23.056 1.000 22.07 ATOM 765 CB ASP A 119 86.197 3.806 23.000 1.000 22.13 ATOM 766 CG ASP A 119 87.190 3.829 21.848 1.000 25.42 ATOM 767 OD1 ASP A 119 87.869 2.807 21.639 1.000 36.77 ATOM 768 OD2 ASP A 119 87.287 4.870 21.172 1.000 26.49 ATOM 769 C ASP A 119 84.094 4.920 23.796 1.000 27.63 ATOM 770 O ASP A 119 83.030 4.908 23.177 1.000 24.16 ATOM 771 N VAL A 120 84.143 4.769 25.119 1.000 24.76 ATOM 772 CA VAL A 120 82.887 4.553 25.842 1.000 22.84 ATOM 773 CB VAL A 120 83.139 4.070 27.282 1.000 22.77 ATOM 774 CG1 VAL A 120 81.837 3.978 28.060 1.000 21.91 ATOM 775 CG2 VAL A 120 83.836 2.719 27.288 1.000 25.70 ATOM 776 C VAL A 120 82.027 5.809 25.873 1.000 18.91 ATOM 777 O VAL A 120 80.851 5.772 25.508 1.000 24.20 ATOM 778 N ASN A 121 82.591 6.929 26.299 1.000 16.61 ATOM 779 CA ASN A 121 81.133 8.133 26.575 1.000 18.33 ATOM 780 CB ASN A 121 82.687 9.131 27.370 1.000 21.37 ATOM 781 CG ASN A 121 82.845 8.766 28.830 1.000 25.63 ATOM 782 OD1 ASN A 121 82.362 7.733 29.286 1.000 24.93 ATOM 783 ND2 ASN A 121 83.530 9.649 29.554 1.000 20.70 ATOM 784 C ASN A 121 81.327 8.853 25.325 1.000 19.73 ATOM 785 O ASN A 121 80.194 9.344 25.345 1.000 20.54 ATOM 786 N LEU A 122 82.173 8.935 24.309 1.000 21.10 ATOM 787 CA LEU A 122 81.869 9.718 23.115 1.000 18.45 ATOM 788 CB LEU A 122 83.085 10.545 22.703 1.000 19.01 ATOM 789 CG LEU A 122 82.961 11.441 21.473 1.000 21.55 ATOM 790 CD1 LEU A 122 81.614 12.151 21.431 1.000 19.41 ATOM 791 CD2 LEU A 122 84.086 12.461 21.448 1.000 15.87 ATOM 792 C LEU A 122 81.422 8.826 21.968 1.000 22.39 ATOM 793 O LEU A 122 80.294 8.948 21.478 1.000 26.80 ATOM 794 N MET A 123 82.287 7.917 21.519 1.000 20.44 ATOM 795 CA MET A 123 81.888 7.004 20.445 1.000 21.80 ATOM 796 CB MET A 123 83.060 6.098 20.072 1.000 21.27 ATOM 797 CG MET A 123 82.766 5.105 18.953 1.000 25.44 ATOM 798 SD MET A 123 82.185 3.504 19.564 1.000 31.17 ATOM 799 CE MET A 123 83.722 2.836 20.210 1.000 23.57 ATOM 800 C MET A 123 80.668 6.186 20.853 1.000 26.48 ATOM 801 O MET A 123 79.736 5.992 20.064 1.000 25.13 ATOM 802 N GLY A 124 80.656 5.705 22.094 1.000 22.35 ATOM 803 CA GLY A 124 79.550 4.901 22.591 1.000 23.21 ATOM 804 C GLY A 124 78.229 5.642 22.491 1.000 27.27 ATOM 805 O GLY A 124 77.207 5.078 22.095 1.000 23.57 ATOM 806 N THR A 125 78.256 6.925 22.860 1.000 22.28 ATOM 807 CA THR A 125 77.045 7.739 22.795 1.000 19.72 ATOM 808 CB THR A 125 77.255 9.070 23.532 1.000 19.88 ATOM 809 OG1 THR A 125 77.070 8.852 24.945 1.000 22.47 ATOM 810 CG2 THR A 125 76.220 10.106 23.132 1.000 18.39 ATOM 811 C THR A 125 76.625 7.967 21.343 1.000 22.09 ATOM 812 O THR A 125 75.439 7.913 21.004 1.000 22.22 ATOM 813 N PHE A 126 77.573 8.233 20.443 1.000 21.93 ATOM 814 CA PHE A 126 77.185 8.425 19.041 1.000 23.53 ATOM 815 CB PHE A 126 78.343 8.986 18.210 1.000 18.23 ATOM 816 CG PHE A 126 77.956 9.204 16.748 1.000 26.47 ATOM 817 CD1 PHE A 126 77.173 10.285 16.374 1.000 23.71 ATOM 818 CD2 PHE A 126 78.369 8.314 15.770 1.000 28.65 ATOM 819 CE1 PHE A 126 76.824 10.480 15.052 1.000 20.77 ATOM 820 CE2 PHE A 126 78.048 8.518 14.439 1.000 25.27 ATOM 821 CZ PHE A 126 77.273 9.604 14.708 1.000 21.02 ATOM 822 C PHE A 126 76.694 7.114 18.432 1.000 21.88 ATOM 823 O PHE A 126 75.783 7.138 17.606 1.000 21.58 ATOM 824 N ASN A 127 77.261 5.979 18.820 1.000 21.02 ATOM 825 CA ASN A 127 76.759 4.686 18.354 1.000 24.14 ATOM 826 CB ASN A 127 77.568 3.521 18.926 1.000 22.79 ATOM 827 CG ASN A 127 77.317 2.205 18.218 1.000 28.53 ATOM 828 OD1 ASN A 127 77.052 2.133 17.017 1.000 29.14 ATOM 829 ND2 ASN A 127 77.406 1.109 18.966 1.000 23.91 ATOM 830 C ASN A 127 75.295 4.488 18.729 1.000 25.90 ATOM 831 O ASN A 127 74.490 4.051 17.904 1.000 28.86 ATOM 832 N VAL A 128 74.942 4.799 19.979 1.000 24.12 ATOM 833 CA VAL A 128 73.540 4.664 20.384 1.000 23.40 ATOM 834 CB VAL A 128 73.350 4.890 21.893 1.000 24.92 ATOM 835 CG1 VAL A 128 71.874 4.993 22.246 1.000 20.34 ATOM 836 CG2 VAL A 128 74.007 3.759 22.670 1.000 22.63 ATOM 837 C VAL A 128 72.672 5.641 19.595 1.000 25.23 ATOM 838 O VAL A 128 71.566 5.294 19.159 1.000 26.49 ATOM 839 N ILE A 129 73.189 6.861 19.429 1.000 20.97 ATOM 840 CA ILE A 129 72.408 7.892 18.747 1.000 21.24 ATOM 841 CB ILE A 129 73.136 9.249 18.751 1.000 20.96 ATOM 842 CG2 ILE A 129 72.554 10.167 17.682 1.000 17.73 ATOM 843 CG1 ILE A 129 73.138 9.927 20.124 1.000 17.73 ATOM 844 CD1 ILE A 129 73.850 11.258 20.195 1.000 19.83 ATOM 845 C ILE A 129 72.092 7.495 17.314 1.000 23.42 ATOM 846 O ILE A 129 70.950 7.589 16.864 1.000 24.98 ATOM 847 N ARG A 130 73.100 7.041 16.577 1.000 22.21 ATOM 848 CA ARG A 130 72.896 6.800 15.146 1.000 23.59 ATOM 849 CB ARG A 130 74.246 6.567 14.467 1.000 21.91 ATOM 850 CG ARG A 130 74.743 5.138 14.544 1.000 20.59 ATOM 851 CD ARG A 130 76.260 5.024 14.349 1.000 20.58 ATOM 852 CZ ARG A 130 76.675 3.671 14.727 1.000 25.06 ATOM 853 NE ARG A 130 76.637 2.621 13.913 1.000 26.85 ATOM 854 NH1 ARG A 130 77.028 1.433 14.360 1.000 23.90 ATOM 855 NH2 ARG A 130 76.220 2.741 12.659 1.000 20.62 ATOM 856 C ARG A 130 71.944 5.632 14.904 1.000 28.92 ATOM 857 O ARG A 130 71.179 5.628 13.932 1.000 23.14 ATOM 858 N LEU A 131 71.989 4.638 15.783 1.000 25.17 ATOM 859 CA LEU A 131 71.155 3.452 15.636 1.000 26.41 ATOM 860 CB LEU A 131 71.766 2.270 16.394 1.000 25.84 ATOM 861 CG LEU A 131 73.124 1.753 15.921 1.000 28.03 ATOM 862 CD1 LEU A 131 73.678 0.706 16.878 1.000 31.36 ATOM 863 CD2 LEU A 131 73.010 1.186 14.512 1.000 32.31 ATOM 864 C LEU A 131 69.730 3.723 16.110 1.000 28.46 ATOM 865 O LEU A 131 68.749 3.359 15.463 1.000 24.94 ATOM 866 N VAL A 132 69.582 4.386 17.257 1.000 22.13 ATOM 867 CA VAL A 132 68.250 4.675 17.733 1.000 18.99 ATOM 868 CB VAL A 132 68.258 5.172 19.228 1.000 22.45 ATOM 869 CG1 VAL A 132 68.598 6.653 19.308 1.000 22.79 ATOM 870 CG2 VAL A 132 66.902 4.903 19.873 1.000 23.15 ATOM 871 C VAL A 132 67.548 5.705 16.896 1.000 23.29 ATOM 872 O VAL A 132 66.314 5.691 16.833 1.000 28.24 ATOM 873 N ALA A 133 68.292 6.586 16.229 1.000 20.41 ATOM 874 CA ALA A 133 67.650 7.522 15.304 1.000 23.10 ATOM 875 CB ALA A 133 68.671 8.475 14.697 1.000 21.23 ATOM 876 C ALA A 133 66.891 6.777 14.209 1.000 24.68 ATOM 877 O ALA A 133 68.772 7.133 13.844 1.000 23.73 ATOM 878 N GLY A 134 67.494 5.719 13.666 1.000 27.05 ATOM 879 CA GLY A 134 66.830 4.933 12.634 1.000 31.03 ATOM 880 C GLY A 134 65.602 4.225 13.168 1.000 34.82 ATOM 881 O GLY A 134 64.647 3.969 12.436 1.000 33.45 ATOM 882 N GLU A 135 65.593 3.877 14.455 1.000 32.85 ATOM 883 CA GLU A 135 64.406 3.276 15.056 1.000 28.48 ATOM 884 CB GLU A 135 64.737 2.662 16.414 1.000 27.36 ATOM 885 CG GLU A 135 65.749 1.534 16.374 1.000 30.53 ATOM 886 CD GLU A 135 65.173 0.289 15.721 1.000 35.24 ATOM 887 OE1 GLU A 135 65.894 −0.377 14.955 1.000 46.65 ATOM 888 OE1 GLU A 135 63.990 −0.011 15.987 1.000 45.16 ATOM 889 C GLU A 135 63.300 4.312 15.218 1.000 28.72 ATOM 890 O GLU A 135 62.128 4.062 14.943 1.000 30.55 ATOM 891 N MET A 136 63.662 5.510 15.681 1.000 22.47 ATOM 892 CA MET A 136 62.637 6.534 15.868 1.000 22.92 ATOM 893 CB MET A 136 63.185 7.726 16.656 1.000 25.85 ATOM 894 CG MET A 136 63.669 7.411 18.066 1.000 28.30 ATOM 895 SD MET A 136 64.718 8.715 18.754 1.000 25.89 ATOM 896 CE MET A 136 64.988 8.067 20.408 1.000 23.78 ATOM 897 C MET A 136 62.095 6.992 14.519 1.000 21.98 ATOM 898 O MET A 136 60.937 7.374 14.392 1.000 28.43 ATOM 899 N GLY A 137 62.925 6.971 13.477 1.000 24.89 ATOM 900 CA GLY A 137 62.492 7.463 12.174 1.000 28.70 ATOM 901 C GLY A 137 61.344 6.642 11.616 1.000 33.98 ATOM 902 O GLY A 137 60.627 7.094 10.717 1.000 35.20 ATOM 903 N GLN A 138 61.158 5.439 12.134 1.000 28.41 ATOM 904 CA GLN A 138 60.034 4.585 11.795 1.000 29.57 ATOM 905 CB GLN A 138 60.413 3.124 12.014 1.000 33.29 ATOM 906 C GLN A 138 58.798 4.942 12.606 1.000 33.23 ATOM 907 O GLN A 138 57.700 4.431 12.349 1.000 36.19 ATOM 908 N ASN A 139 58.901 5.817 13.613 1.000 30.84 ATOM 909 CA ASN A 139 57.673 6.225 14.290 1.000 29.71 ATOM 910 CB ASN A 139 57.951 6.918 15.616 1.000 30.72 ATOM 911 CG ASN A 139 58.539 6.044 16.695 1.000 34.82 ATOM 912 OD1 ASN A 139 58.309 4.840 16.748 1.000 33.24 ATOM 913 ND2 ASN A 139 59.316 6.643 17.599 1.000 27.65 ATOM 914 C ASN A 139 56.873 7.178 13.405 1.000 32.55 ATOM 915 O ASN A 139 57.442 7.999 12.686 1.000 31.43 ATOM 916 N GLU A 140 55.545 7.095 13.455 1.000 32.34 ATOM 917 CA GLU A 140 54.765 8.130 12.765 1.000 33.47 ATOM 918 CB GLU A 140 53.338 7.698 12.521 1.000 37.78 ATOM 919 C GLU A 140 54.829 9.390 13.622 1.000 33.02 ATOM 920 O GLU A 140 54.685 9.297 14.848 1.000 31.57 ATOM 921 N PRO A 141 55.053 10.552 13.029 1.000 31.82 ATOM 922 CD PRO A 141 55.197 10.833 11.595 1.000 30.12 ATOM 923 CA PRO A 141 55.180 11.763 13.850 1.000 30.60 ATOM 924 CB PRO A 141 55.411 12.868 12.821 1.000 32.30 ATOM 925 CG PRO A 141 55.887 12.174 11.595 1.000 31.21 ATOM 926 C PRO A 141 53.892 12.026 14.618 1.000 37.04 ATOM 927 O PRO A 141 52.792 11.743 14.141 1.000 38.85 ATOM 928 N ASP A 142 54.021 12.576 15.821 1.000 32.62 ATOM 929 CA ASP A 142 52.834 13.005 16.551 1.000 30.09 ATOM 930 CB ASP A 142 53.157 13.277 18.011 1.000 33.63 ATOM 931 CG ASP A 142 54.244 14.306 18.230 1.000 34.93 ATOM 932 OD1 ASP A 142 54.390 15.234 17.410 1.000 25.78 ATOM 933 OD2 ASP A 142 54.970 14.201 19.245 1.000 35.97 ATOM 934 C ASP A 142 52.264 14.255 15.881 1.000 35.02 ATOM 935 O ASP A 142 52.772 14.699 14.848 1.000 29.85 ATOM 936 N GLN A 143 51.224 14.806 16.494 1.000 33.99 ATOM 937 CA GLN A 143 50.579 16.007 15.990 1.000 38.09 ATOM 938 CB GLN A 143 49.401 16.380 16.884 1.000 38.12 ATOM 939 C GLN A 143 51.547 17.178 15.890 1.000 40.07 ATOM 940 O GLN A 143 51.283 18.129 15.148 1.000 37.88 ATOM 941 N GLY A 144 52.656 17.131 16.625 1.000 34.69 ATOM 942 CA GLY A 144 53.618 18.218 16.584 1.000 30.50 ATOM 943 C GLY A 144 54.788 17.941 15.657 1.000 30.57 ATOM 944 O GLY A 144 55.778 18.668 15.666 1.000 30.79 ATOM 945 N GLY A 145 54.672 16.890 14.857 1.000 28.63 ATOM 946 CA GLY A 145 55.684 16.503 13.902 1.000 26.20 ATOM 947 C GLY A 145 56.793 15.676 14.508 1.000 26.99 ATOM 948 O GLY A 145 57.758 15.304 13.841 1.000 25.11 ATOM 949 N GLN A 146 56.698 15.370 15.797 1.000 26.86 ATOM 950 CA GLN A 146 57.832 14.756 16.482 1.000 26.54 ATOM 951 CB GLN A 146 57.877 15.283 17.926 1.000 26.88 ATOM 952 CG GLN A 146 59.203 14.976 18.615 1.000 31.74 ATOM 953 CD GLN A 146 59.200 15.449 20.057 1.000 29.31 ATOM 954 OE1 GLN A 146 59.518 16.613 20.289 1.000 27.82 ATOM 955 NE2 GLN A 146 58.846 14.565 20.986 1.000 26.30 ATOM 956 C GLN A 146 57.794 13.239 16.479 1.000 27.53 ATOM 957 O GLN A 146 56.743 12.629 16.690 1.000 29.32 ATOM 958 N ARG A 147 58.957 12.634 16.643 1.000 22.43 ATOM 959 CA ARG A 147 59.134 11.200 16.208 1.000 20.85 ATOM 960 CB ARG A 147 59.862 10.761 14.937 1.000 22.13 ATOM 961 CG ARG A 147 59.043 10.766 13.663 1.000 23.35 ATOM 962 CD ARG A 147 59.897 10.222 12.520 1.000 26.83 ATOM 963 NE ARG A 147 59.101 10.004 11.309 1.000 28.18 ATOM 964 CZ ARG A 147 59.049 10.883 10.313 1.000 32.45 ATOM 965 NH1 ARG A 147 58.306 10.621 9.246 1.000 37.01 ATOM 966 NH2 ARG A 147 59.736 12.015 10.385 1.000 28.29 ATOM 967 C ARG A 147 59.968 10.684 17.380 1.000 27.24 ATOM 968 O ARG A 147 59.901 9.498 17.710 1.000 25.10 ATOM 969 N GLY A 148 60.776 11.548 17.994 1.000 25.61 ATOM 970 CA GLY A 148 61.684 11.059 19.019 1.000 24.15 ATOM 971 C GLY A 148 62.366 12.198 19.761 1.000 25.59 ATOM 972 O GLY A 148 62.322 13.322 19.276 1.000 22.65 ATOM 973 N VAL A 149 62.915 11.884 20.929 1.000 23.40 ATOM 974 CA VAL A 149 63.767 12.768 21.704 1.000 22.36 ATOM 975 CB VAL A 149 63.054 13.362 22.930 1.000 22.74 ATOM 976 CG1 VAL A 149 63.922 14.438 23.584 1.000 25.25 ATOM 977 CG2 VAL A 149 61.703 13.937 22.539 1.000 29.65 ATOM 978 C VAL A 149 65.016 12.010 22.150 1.000 22.55 ATOM 979 O VAL A 149 64.954 10.907 22.666 1.000 20.35 ATOM 980 N ILE A 150 66.183 12.602 21.951 1.000 24.00 ATOM 981 CA ILE A 150 67.442 12.020 22.398 1.000 22.32 ATOM 982 CB ILE A 150 68.377 11.695 21.220 1.000 24.31 ATOM 983 CG2 ILE A 150 69.729 11.203 21.721 1.000 22.61 ATOM 984 CG1 ILE A 150 67.770 10.709 20.223 1.000 21.68 ATOM 985 CD1 ILE A 150 68.649 10.447 19.019 1.000 23.99 ATOM 986 C ILE A 150 68.127 12.991 23.356 1.000 23.92 ATOM 987 O ILE A 150 68.657 14.172 23.041 1.000 23.96 ATOM 988 N ILE A 151 68.538 12.488 24.512 1.000 20.89 ATOM 989 CA ILE A 151 69.131 13.304 25.564 1.000 18.19 ATOM 990 CB ILE A 151 68.303 13.414 26.786 1.000 19.91 ATOM 991 CG2 ILE A 151 68.801 14.266 27.888 1.000 15.01 ATOM 992 CG1 ILE A 151 66.808 13.944 26.428 1.000 23.45 ATOM 993 CD1 ILE A 151 65.805 13.843 27.556 1.000 24.66 ATOM 994 C ILE A 151 70.462 12.689 25.972 1.000 21.60 ATOM 995 O ILE A 151 70.484 11.519 26.366 1.000 22.74 ATOM 996 N ASN A 152 71.524 13.476 25.847 1.000 20.63 ATOM 997 CA ASN A 152 72.867 12.980 26.113 1.000 18.99 ATOM 998 CB ASN A 152 73.836 13.384 24.992 1.000 19.22 ATOM 999 CG ASN A 152 73.211 13.074 23.637 1.000 20.09 ATOM 1000 OD1 ASN A 152 72.912 13.977 22.856 1.000 33.18 ATOM 1001 ND2 ASN A 152 73.017 11.795 23.386 1.000 15.75 ATOM 1002 C ASN A 152 73.395 13.517 27.437 1.000 22.55 ATOM 1003 O ASN A 152 72.860 14.512 27.943 1.000 21.43 ATOM 1004 N THR A 153 74.438 12.854 27.944 1.000 21.33 ATOM 1005 CA THR A 153 75.076 13.367 29.150 1.000 19.67 ATOM 1006 CB THR A 153 75.042 12.363 30.311 1.000 20.60 ATOM 1007 OG1 THR A 153 73.730 11.801 30.437 1.000 20.29 ATOM 1008 CG2 THR A 153 75.315 13.093 31.620 1.000 20.24 ATOM 1009 C THR A 153 76.520 13.771 28.857 1.000 20.09 ATOM 1010 O THR A 153 77.336 12.925 28.497 1.000 20.49 ATOM 1011 N ALA A 154 76.797 15.058 29.012 1.000 17.99 ATOM 1012 CA ALA A 154 78.157 15.580 28.941 1.000 21.71 ATOM 1013 CB ALA A 154 78.230 16.698 28.183 1.000 15.72 ATOM 1014 C ALA A 154 78.678 15.745 30.366 1.000 18.97 ATOM 1015 O ALA A 154 78.650 14.795 31.141 1.000 21.19 ATOM 1016 N SER A 155 79.124 16.935 30.721 1.000 22.57 ATOM 1017 CA SER A 155 79.663 17.252 32.041 1.000 19.46 ATOM 1018 CB SER A 155 80.837 16.336 32.389 1.000 20.68 ATOM 1019 OG SER A 155 81.569 16.832 33.512 1.000 19.92 ATOM 1020 C SER A 155 80.132 18.969 32.066 1.000 19.44 ATOM 1021 O SER A 155 80.451 19.246 31.008 1.000 18.95 ATOM 1022 N VAL A 156 80.226 19.329 33.240 1.000 17.21 ATOM 1023 CA VAL A 156 80.827 20.659 33.282 1.000 16.12 ATOM 1024 CB VAL A 156 80.606 21.359 34.638 1.000 22.05 ATOM 1025 CG1 VAL A 156 79.111 21.526 34.908 1.000 23.71 ATOM 1026 CG2 VAL A 156 81.286 20.596 35.758 1.000 23.52 ATOM 1027 C VAL A 156 82.320 20.593 32.977 1.000 15.83 ATOM 1028 O VAL A 156 82.948 21.638 32.780 1.000 18.99 ATOM 1029 N ALA A 157 82.900 19.397 32.941 1.000 17.17 ATOM 1030 CA ALA A 157 84.294 19.227 35.522 1.000 17.12 ATOM 1031 CB ALA A 157 84.783 17.824 32.831 1.000 14.53 ATOM 1032 C ALA A 157 84.460 19.540 31.038 1.000 21.86 ATOM 1033 O ALA A 157 85.573 19.705 30.542 1.000 22.45 ATOM 1034 N ALA A 158 83.369 19.638 30.292 1.000 21.67 ATOM 1035 CA ALA A 158 83.424 20.098 28.902 1.000 21.61 ATOM 1036 CB ALA A 158 82.081 19.902 28.225 1.000 18.71 ATOM 1037 C ALA A 158 83.835 21.561 28.856 1.000 21.63 ATOM 1038 O ALA A 158 84.331 22.076 27.858 1.000 21.79 ATOM 1039 N PHE A 159 83.621 22.268 22.969 1.000 18.53 ATOM 1040 CA PHE A 159 83.861 23.702 30.013 1.000 21.39 ATOM 1041 CB PHE A 159 82.558 24.436 30.386 1.000 22.21 ATOM 1042 CG PHE A 159 81.370 24.032 29.536 1.000 23.73 ATOM 1043 CD1 PHE A 159 80.333 23.289 30.067 1.000 23.69 ATOM 1044 CD2 PHE A 159 81.317 24.402 28.204 1.000 24.10 ATOM 1045 CE1 PHE A 159 79.251 22.908 29.283 1.000 23.62 ATOM 1046 CE2 PHE A 159 80.237 24.032 27.419 1.000 26.19 ATOM 1047 CZ PHE A 159 79.204 23.293 27.960 1.000 22.24 ATOM 1048 C PHE A 159 84.949 21.110 30.997 1.000 24.75 ATOM 1049 O PHE A 159 85.636 25.110 30.780 1.000 22.24 ATOM 1050 N GLU A 160 85.118 23.285 32.097 1.000 22.83 ATOM 1051 CA GLU A 160 86.123 23.705 33.102 1.000 24.53 ATOM 1052 CB GLU A 160 85.536 24.348 34.355 1.000 26.40 ATOM 1053 CG GLU A 160 84.785 25.647 34.193 1.000 31.12 ATOM 1054 CD GLU A 160 83.296 25.519 34.442 1.000 34.00 ATOM 1055 OE1 GLU A 160 82.527 26.110 33.652 1.000 30.58 ATOM 1056 OE2 GLU A 160 82.858 24.845 35.397 1.000 25.33 ATOM 1057 C GLU A 160 86.865 22.434 33.526 1.000 22.82 ATOM 1058 O GLU A 160 86.876 22.118 34.722 1.000 22.77 ATOM 1059 N GLY A 161 87.450 21.730 32.560 1.000 17.77 ATOM 1060 CA GLY A 161 88.190 20.511 32.844 1.000 20.11 ATOM 1061 C GLY A 161 89.207 20.771 33.988 1.000 22.40 ATOM 1062 O GLY A 161 89.925 21.771 33.954 1.000 19.29 ATOM 1063 N GLN A 162 89.250 19.898 34.986 1.000 21.52 ATOM 1064 CA GLN A 162 90.173 20.050 36.106 1.000 24.64 ATOM 1065 CB GLN A 162 89.554 19.454 37.375 1.000 21.82 ATOM 1066 CG GLN A 162 88.342 20.197 37.909 1.000 23.34 ATOM 1067 CD GLN A 162 88.026 19.778 39.341 1.000 25.33 ATOM 1068 OE1 GLN A 162 87.431 18.723 39.550 1.000 25.69 ATOM 1069 NE2 GLN A 162 88.428 20.600 40.306 1.000 21.01 ATOM 1070 C GLN A 162 91.495 19.343 35.833 1.000 24.73 ATOM 1071 O GLN A 162 91.586 18.564 34.881 1.000 21.61 ATOM 1072 N VAL A 163 92.483 19.598 36.690 1.000 22.60 ATOM 1073 CA VAL A 163 93.739 18.841 36.572 1.000 22.73 ATOM 1074 CB VAL A 163 94.752 19.204 37.667 1.000 20.09 ATOM 1075 CG1 VAL A 163 95.932 18.237 37.643 1.000 22.25 ATOM 1076 CG2 VAL A 163 95.233 20.641 37.504 1.000 14.78 ATOM 1077 C VAL A 163 93.436 17.350 36.637 1.000 23.33 ATOM 1078 O VAL A 163 92.734 16.916 37.552 1.000 26.46 ATOM 1079 N GLY A 164 93.925 16.560 35.692 1.000 20.35 ATOM 1080 CA GLY A 164 93.645 15.138 35.560 1.000 19.48 ATOM 1081 C GLY A 164 92.459 14.754 34.783 1.000 23.54 ATOM 1082 O GLY A 164 92.222 13.560 34.572 1.000 22.45 ATOM 1083 N GLN A 165 91.689 15.709 34.263 1.000 21.33 ATOM 1084 CA GLN A 165 90.485 15.381 33.506 1.000 22.94 ATOM 1085 CB GLN A 165 89.313 16.245 33.986 1.000 22.47 ATOM 1086 CG GLN A 165 88.735 15.870 35.337 1.000 26.75 ATOM 1087 CD GLN A 165 87.425 16.603 35.591 1.000 28.68 ATOM 1088 OE1 GLN A 165 87.305 17.805 35.337 1.000 24.50 ATOM 1089 NE2 GLN A 165 86.442 15.866 36.091 1.000 28.31 ATOM 1090 C GLN A 165 90.598 15.595 32.002 1.000 25.31 ATOM 1091 O GLN A 165 89.564 31.325 31.325 1.000 24.16 ATOM 1092 N ALA A 166 91.795 15.645 31.432 1.000 20.17 ATOM 1093 CA ALA A 166 91.934 15.880 29.992 1.000 19.87 ATOM 1094 CB ALA A 166 93.411 15.881 29.620 1.000 21.17 ATOM 1095 C ALA A 166 91.166 14.870 29.156 1.000 22.80 ATOM 1096 O ALA A 166 90.404 15.240 28.254 1.000 23.88 ATOM 1097 N ALA A 167 91.325 13.572 29.410 1.000 20.76 ATOM 1098 CA ALA A 167 90.598 12.576 28.619 1.000 18.57 ATOM 1099 CB ALA A 167 91.081 11.188 28.998 1.000 20.24 ATOM 1100 C ALA A 167 89.093 12.682 28.810 1.000 22.84 ATOM 1101 O ALA A 167 88.305 12.642 27.866 1.000 21.97 ATOM 1102 N TYR A 168 88.644 12.808 30.059 1.000 19.71 ATOM 1103 CA TYR A 168 87.244 12.964 30.346 1.000 18.72 ATOM 1104 CB TYR A 168 86.990 13.100 31.854 1.000 19.50 ATOM 1105 CG TYR A 168 85.552 12.961 32.315 1.000 17.69 ATOM 1106 CD1 TYR A 168 84.865 11.762 32.189 1.000 19.32 ATOM 1107 CE1 TYR A 168 83.554 11.634 32.611 1.000 19.30 ATOM 1108 CD2 TYR A 168 84.887 14.038 32.890 1.000 16.32 ATOM 1109 CE2 TYR A 168 83.574 13.929 33.324 1.000 18.41 ATOM 1110 CZ TYR A 168 82.919 12.724 33.181 1.000 22.12 ATOM 1111 OH TYR A 168 81.616 12.584 33.603 1.000 21.21 ATOM 1112 C TYR A 168 86.651 14.186 29.630 1.000 21.33 ATOM 1113 O TYR A 168 85.593 14.116 29.009 1.000 21.12 ATOM 1114 N SER A 169 87.367 15.294 29.741 1.000 18.05 ATOM 1115 CA SER A 169 86.938 16.572 29.194 1.000 17.88 ATOM 1116 CB SER A 169 87.876 17.706 29.606 1.000 19.40 ATOM 1117 OG SER A 169 87.889 17.932 31.008 1.000 20.81 ATOM 1118 C SER A 169 86.848 16.499 27.667 1.000 22.37 ATOM 1119 O SER A 169 85.950 17.101 27.079 1.000 22.30 ATOM 1120 N ALA A 170 87.787 15.770 27.080 1.000 21.43 ATOM 1121 CA ALA A 170 87.820 15.524 25.643 1.000 20.27 ATOM 1122 CB ALA A 170 89.051 14.700 25.279 1.000 17.19 ATOM 1123 C ALA A 170 86.552 14.801 25.203 1.000 23.52 ATOM 1124 O ALA A 170 85.894 15.162 24.229 1.000 21.45 ATOM 1125 N SER A 171 86.204 13.754 25.947 1.000 18.86 ATOM 1126 CA SER A 171 85.032 12.950 25.622 1.000 17.10 ATOM 1127 CB SER A 171 85.051 11.681 26.473 1.000 18.30 ATOM 1128 OG SER A 171 84.557 11.914 27.786 1.000 22.04 ATOM 1129 C SER A 171 83.740 13.735 25.811 1.000 22.12 ATOM 1130 O SER A 171 82.803 13.603 25.015 1.000 23.65 ATOM 1131 N LYS A 172 83.668 14.564 26.858 1.000 17.81 ATOM 1132 CA LYS A 172 82.442 15.323 27.110 1.000 20.04 ATOM 1133 CB LYS A 172 82.330 15.703 28.592 1.000 18.29 ATOM 1134 CG LYS A 172 82.267 14.485 29.505 1.000 17.34 ATOM 1135 CD LYS A 172 81.143 13.533 29.128 1.000 21.47 ATOM 1136 CE LYS A 172 80.971 12.469 30.211 1.000 19.97 ATOM 1137 NZ LYS A 172 79.740 11.651 30.012 1.000 16.10 ATOM 1138 C LYS A 172 82.365 16.563 26.232 1.000 21.83 ATOM 1139 O LYS A 172 81.282 16.962 25.804 1.000 20.78 ATOM 1140 N GLY A 173 83.501 17.189 25.934 1.000 20.14 ATOM 1141 CA GLY A 173 83.504 18.311 25.002 1.000 19.14 ATOM 1142 C GLY A 173 83.042 17.843 23.623 1.000 22.28 ATOM 1143 O GLY A 173 82.382 18.601 22.905 1.000 20.41 ATOM 1144 N GLY A 174 83.399 16.599 23.295 1.000 18.15 ATOM 1145 CA GLY A 174 82.918 15.952 22.083 1.000 19.24 ATOM 1146 C GLY A 174 81.397 15.897 22.049 1.000 23.10 ATOM 1147 O GLY A 174 80.746 16.228 21.053 1.000 18.74 ATOM 1148 N ILE A 175 80.801 15.470 23.165 1.000 23.71 ATOM 1149 CA ILE A 175 79.344 15.374 23.240 1.000 18.13 ATOM 1150 CB ILE A 175 78.859 14.808 24.585 1.000 22.59 ATOM 1151 CG2 ILE A 175 77.333 14.772 24.601 1.000 19.28 ATOM 1152 CG1 ILE A 175 79.439 13.444 24.954 1.000 21.35 ATOM 1153 CD1 ILE A 175 78.870 12.312 24.142 1.000 29.59 ATOM 1154 C ILE A 175 78.710 16.741 23.050 1.000 20.98 ATOM 1155 O ILE A 175 77.720 16.959 22.343 1.000 22.66 ATOM 1156 N VAL A 176 79.321 17.723 23.727 1.000 14.93 ATOM 1157 CA VAL A 176 78.799 19.079 23.568 1.000 13.95 ATOM 1158 CB VAL A 176 79.535 20.078 24.467 1.000 20.03 ATOM 1159 CG1 VAL A 176 79.154 21.504 24.109 1.000 18.47 ATOM 1160 CG2 VAL A 176 79.229 19.794 25.936 1.000 18.79 ATOM 1161 C VAL A 176 78.897 19.488 22.105 1.000 19.79 ATOM 1162 O VAL A 176 77.916 19.919 21.505 1.000 20.43 ATOM 1163 N GLY A 177 80.074 19.348 21.490 1.000 20.46 ATOM 1164 CA GLY A 177 80.236 19.823 20.125 1.000 20.42 ATOM 1165 C GLY A 177 79.334 19.148 19.115 1.000 23.30 ATOM 1166 O GLY A 177 78.913 19.781 18.138 1.000 22.67 ATOM 1167 N MET A 178 78.997 17.869 19.277 1.000 19.64 ATOM 1168 CA MET A 178 78.174 17.239 18.244 1.000 18.59 ATOM 1169 CB MET A 178 78.527 15.754 18.109 1.000 18.46 ATOM 1170 CG MET A 178 78.124 14.883 19.283 1.000 21.01 ATOM 1171 SD MET A 178 78.675 13.176 19.081 1.000 24.29 ATOM 1172 CE MET A 178 77.901 12.383 20.486 1.000 18.63 ATOM 1173 C MET A 178 76.677 17.381 18.498 1.000 21.98 ATOM 1174 O MET A 178 75.854 16.917 17.703 1.000 22.55 ATOM 1175 N THR A 179 76.303 18.020 19.601 1.000 18.53 ATOM 1176 CA THR A 179 74.882 18.192 19.915 1.000 18.51 ATOM 1177 CB THR A 179 74.719 18.925 21.266 1.000 19.84 ATOM 1178 OG1 THR A 179 75.155 18.062 22.331 1.000 18.46 ATOM 1179 CG2 THR A 179 73.261 19.271 21.537 1.000 15.79 ATOM 1180 C THR A 179 74.148 18.940 18.813 1.000 23.20 ATOM 1181 O THR A 179 73.114 18.480 18.315 1.000 21.33 ATOM 1182 N LEU A 180 74.649 20.099 18.396 1.000 21.40 ATOM 1183 CA LEU A 180 73.940 20.900 17.400 1.000 20.22 ATOM 1184 CB LEU A 180 74.563 22.297 17.303 1.000 17.06 ATOM 1185 CG LEU A 180 73.884 23.245 16.308 1.000 23.58 ATOM 1186 CD1 LEU A 180 72.454 23.531 16.740 1.000 24.53 ATOM 1187 CD2 LEU A 180 74.683 24.531 16.158 1.000 21.92 ATOM 1188 C LEU A 180 73.906 20.253 16.020 1.000 18.83 ATOM 1189 O LEU A 180 72.827 20.176 15.421 1.000 22.66 ATOM 1190 N PRO A 181 75.022 19.807 15.460 1.000 20.32 ATOM 1191 CD PRO A 181 76.403 19.915 15.952 1.000 19.33 ATOM 1192 CA PRO A 181 74.976 19.137 14.148 1.000 20.68 ATOM 1193 CB PRO A 181 76.411 18.645 13.926 1.000 22.44 ATOM 1194 CG PRO A 181 77.074 18.748 15.264 1.000 20.59 ATOM 1195 C PRO A 181 74.034 17.943 14.120 1.000 27.41 ATOM 1196 O PRO A 181 73.304 17.744 13.139 1.000 22.18 ATOM 1197 N ILE A 182 74.023 17.111 15.168 1.000 20.68 ATOM 1198 CA ILE A 182 73.095 15.976 15.144 1.000 18.87 ATOM 1199 CB ILE A 182 73.354 14.981 16.283 1.000 18.97 ATOM 1200 CG2 ILE A 182 72.317 13.868 16.266 1.000 19.51 ATOM 1201 CG1 ILE A 182 74.760 14.380 16.254 1.000 19.27 ATOM 1202 CD1 ILE A 182 75.128 13.520 17.437 1.000 20.55 ATOM 1203 C ILE A 182 74.660 16.499 15.170 1.000 23.55 ATOM 1204 O ILE A 182 70.825 16.022 14.398 1.000 23.85 ATOM 1205 N ALA A 183 71.390 17.490 16.026 1.000 19.15 ATOM 1206 CA ALA A 183 70.071 18.126 16.012 1.000 20.67 ATOM 1207 CB ALA A 183 70.005 19.247 17.039 1.000 20.13 ATOM 1208 C ALA A 183 69.758 18.656 14.611 1.000 25.01 ATOM 1209 O ALA A 183 68.653 18.519 14.087 1.000 21.56 ATOM 1210 N ARG A 184 70.739 19.287 13.962 1.000 21.73 ATOM 1211 CA ARG A 184 70.485 19.799 12.610 1.000 21.73 ATOM 1212 CB ARG A 184 71.642 20.679 12.134 1.000 17.36 ATOM 1213 CG ARG A 184 71.779 21.973 12.907 1.000 16.93 ATOM 1214 CD ARG A 184 73.039 22.748 12.567 1.000 17.35 ATOM 1215 NE ARG A 184 72.915 24.175 12.842 1.000 21.03 ATOM 1216 CZ ARG A 184 73.838 25.093 12.581 1.000 20.96 ATOM 1217 NH1 ARG A 184 73.645 23.374 12.864 1.000 18.08 ATOM 1218 NH2 ARG A 184 75.000 24.762 12.025 1.000 20.87 ATOM 1219 C ARG A 184 70.038 18.626 11.667 1.000 21.16 ATOM 1220 O ARG A 184 69.317 18.667 10.841 1.000 21.06 ATOM 1221 N ASP A 185 71.030 17.564 11.799 1.000 16.34 ATOM 1222 CA ASP A 185 70.844 16.368 10.987 1.000 19.85 ATOM 1223 CB ASP A 185 71.782 15.251 11.432 1.000 21.41 ATOM 1224 CG ASP A 185 73.175 15.269 10.850 1.000 24.87 ATOM 1225 OD1 ASP A 185 73.959 14.367 11.247 1.000 21.48 ATOM 1226 OD2 ASP A 185 73.527 16.130 10.020 1.000 18.18 ATOM 1227 C ASP A 185 69.419 15.818 11.060 1.000 26.43 ATOM 1228 O ASP A 185 68.808 15.496 10.036 1.000 20.25 ATOM 1229 N LEU A 186 69.893 15.689 12.282 1.000 20.78 ATOM 1230 CA LEU A 186 67.630 14.992 12.483 1.000 20.72 ATOM 1231 CB LEU A 186 67.689 14.210 13.806 1.000 20.73 ATOM 1232 CG LEU A 186 68.918 13.319 13.997 1.000 22.47 ATOM 1233 CD1 LEU A 186 68.781 12.514 15.282 1.000 20.41 ATOM 1234 CD2 LEU A 186 69.120 12.401 12.799 1.000 19.86 ATOM 1235 C LEU A 186 66.411 15.900 12.496 1.000 22.45 ATOM 1236 O LEU A 186 65.263 15.440 12.554 1.000 24.25 ATOM 1237 N ALA A 187 66.624 17.210 12.453 1.000 15.94 ATOM 1238 CA ALA A 187 65.484 18.127 12.463 1.000 18.11 ATOM 1239 CB ALA A 187 65.992 19.563 12.429 1.000 15.41 ATOM 1240 C ALA A 187 64.490 17.852 11.344 1.000 24.07 ATOM 1241 O ALA A 187 63.275 17.911 11.601 1.000 24.26 ATOM 1242 N PRO A 188 64.865 17.560 10.109 1.000 27.53 ATOM 1243 CD PRO A 188 66.210 17.517 9.510 1.000 30.77 ATOM 1244 CA PRO A 188 63.843 17.246 9.097 1.000 28.68 ATOM 1245 CB PRO A 188 64.660 16.872 7.848 1.000 28.47 ATOM 1246 CG PRO A 188 65.927 17.649 8.036 1.000 32.25 ATOM 1247 C PRO A 188 62.971 16.066 9.471 1.000 32.36 ATOM 1248 O PRO A 188 61.897 15.882 8.886 1.000 30.80 ATOM 1249 N ILE A 189 63.381 15.222 10.423 1.000 27.68 ATOM 1250 CA ILE A 189 62.466 14.100 10.677 1.000 27.31 ATOM 1251 CB ILE A 189 63.133 12.746 10.415 1.000 31.22 ATOM 1252 CG2 ILE A 189 63.458 12.582 8.932 1.000 36.22 ATOM 1253 CG1 ILE A 189 64.389 12.443 11.227 1.000 27.19 ATOM 1254 CD1 ILE A 189 64.885 11.011 11.005 1.000 28.72 ATOM 1255 C ILE A 189 61.890 14.171 12.088 1.000 23.39 ATOM 1256 O ILE A 189 61.367 13.198 12.633 1.000 25.26 ATOM 1257 N GLY A 190 61.973 15.530 12.696 1.000 18.90 ATOM 1258 CA GLY A 190 61.345 15.608 13.970 1.000 20.72 ATOM 1259 C GLY A 190 61.925 14.880 15.159 1.000 23.61 ATOM 1260 O GLY A 190 61.202 14.431 16.052 1.000 25.17 ATOM 1261 N ILE A 191 63.248 14.742 15.202 1.000 20.22 ATOM 1262 CA ILE A 191 63.887 14.146 16.375 1.000 20.80 ATOM 1263 CB ILE A 191 64.762 12.938 16.021 1.000 20.20 ATOM 1264 CG2 ILE A 191 62.535 12.457 17.243 1.000 23.67 ATOM 1265 CG1 ILE A 191 63.978 11.784 15.393 1.000 21.41 ATOM 1266 CD1 ILE A 191 64.857 10.645 14.911 1.000 20.93 ATOM 1267 C ILE A 191 64.730 15.216 17.070 1.000 23.22 ATOM 1268 O ILE A 191 65.691 15.702 16.474 1.000 23.95 ATOM 1269 N ARG A 192 64.342 15.563 18.298 1.000 20.33 ATOM 1270 CA ARG A 192 65.063 16.567 19.069 1.000 19.85 ATOM 1271 CB ARG A 192 64.185 17.172 20.169 1.000 20.25 ATOM 1272 CG ARG A 192 63.053 18.031 19.641 1.000 21.19 ATOM 1273 CD ARG A 192 62.285 18.757 20.720 1.000 20.91 ATOM 1274 NE ARG A 192 61.452 17.886 21.554 1.000 21.19 ATOM 1275 CZ ARG A 192 61.635 17.793 22.871 1.000 23.70 ATOM 1276 NH1 ARG A 192 62.597 18.494 23.462 1.000 20.82 ATOM 1277 NH2 ARG A 192 60.869 17.000 23.606 1.000 22.23 ATOM 1278 C ARG A 192 66.308 15.944 19.699 1.000 19.83 ATOM 1279 O ARG A 192 66.281 14.761 20.052 1.000 21.50 ATOM 1280 N VAL A 193 67.352 16.752 19.827 1.000 20.77 ATOM 1281 CA VAL A 193 68.585 16.282 20.464 1.000 21.10 ATOM 1282 CB VAL A 193 69.706 16.014 19.449 1.000 21.95 ATOM 1283 CG1 VAL A 193 70.938 15.439 20.132 1.000 21.45 ATOM 1284 CG2 VAL A 193 69.225 15.065 18.356 1.000 18.83 ATOM 1285 C VAL A 193 69.024 17.321 21.493 1.000 21.27 ATOM 1286 O VAL A 193 69.264 18.476 21.157 1.000 18.26 ATOM 1287 N MET A 194 69.099 16.893 22.746 1.000 20.77 ATOM 1288 CA MET A 194 69.458 17.762 23.856 1.000 20.59 ATOM 1289 CB MET A 194 68.226 18.038 27.719 1.000 21.73 ATOM 1290 CG MET A 194 67.235 19.025 24.121 1.000 20.14 ATOM 1291 SD MET A 194 67.834 20.721 24.138 1.000 21.56 ATOM 1292 CE MET A 194 68.099 20.980 25.905 1.000 16.72 ATOM 1293 C MET A 194 70.561 17.137 24.706 1.000 24.88 ATOM 1294 O MET A 194 70.762 15.918 24.723 1.000 20.06 ATOM 1295 N THR A 195 71.293 17.991 25.431 1.000 23.18 ATOM 1296 CA THR A 195 72.360 17.453 26.281 1.000 21.06 ATOM 1297 CB THR A 195 73.726 17.690 25.615 1.000 20.20 ATOM 1298 OG1 THR A 195 73.807 16.866 24.440 1.000 20.09 ATOM 1299 CG2 THR A 195 74.865 17.267 26.259 1.000 20.65 ATOM 1300 C THR A 195 72.320 18.078 27.668 1.000 19.09 ATOM 1301 O THR A 195 72.095 19.281 27.817 1.000 22.65 ATOM 1302 N ILE A 196 72.531 17.260 28.695 1.000 21.42 ATOM 1303 CA ILE A 196 72.642 17.775 30.054 1.000 21.21 ATOM 1304 CB ILE A 196 71.775 16.991 31.058 1.000 22.86 ATOM 1305 CG2 ILE A 196 72.088 17.388 32.496 1.000 13.56 ATOM 1306 CG1 ILE A 196 70.270 17.101 30.786 1.000 18.56 ATOM 1307 CD1 ILE A 196 69.434 15.969 31.334 1.000 21.74 ATOM 1308 C ILE A 196 74.109 17.727 30.487 1.000 19.78 ATOM 1309 O ILE A 196 74.770 16.720 30.243 1.000 20.85 ATOM 1310 N ALA A 197 74.586 18.798 31.107 1.000 17.33 ATOM 1311 CA ALA A 197 75.910 18.819 31.706 1.000 20.74 ATOM 1312 CB ALA A 197 76.703 20.032 31.236 1.000 15.79 ATOM 1313 C ALA A 197 75.807 18.823 33.232 1.000 17.73 ATOM 1314 O ALA A 197 75.684 19.885 33.844 1.000 20.44 ATOM 1315 N PRO A 198 78.851 17.663 33.859 1.000 15.54 ATOM 1316 CD PRO A 198 75.908 16.311 33.281 1.000 14.44 ATOM 1317 CA PRO A 198 75.815 17.630 35.325 1.000 18.78 ATOM 1318 CB PRO A 198 75.661 16.145 35.650 1.000 18.65 ATOM 1319 CG PRO A 198 75.273 15.478 34.368 1.000 16.32 ATOM 1320 C PRO A 198 77.101 18.178 35.939 1.000 21.23 ATOM 1321 O PRO A 198 78.200 18.050 35.387 1.000 21.65 ATOM 1322 N GLY A 199 76.973 18.801 37.111 1.000 16.71 ATOM 1323 CA GLY A 199 78.144 19.282 37.831 1.000 20.34 ATOM 1324 C GLY A 199 78.720 18.158 38.681 1.000 25.67 ATOM 1325 O GLY A 199 79.558 17.382 38.215 1.000 29.26 ATOM 1326 N LEU A 200 78.276 18.047 39.936 1.000 24.30 ATOM 1327 CA LEU A 200 78.728 16.935 40.779 1.000 24.04 ATOM 1328 CB LEU A 200 79.670 17.423 41.874 1.000 28.95 ATOM 1329 CG LEU A 200 80.780 19.398 41.494 1.000 27.68 ATOM 1330 CD1 LEU A 200 81.456 18.959 42.741 1.000 23.71 ATOM 1331 CD2 LEU A 200 81.833 17.748 40.608 1.000 26.72 ATOM 1332 C LEU A 200 77.516 16.224 41.373 1.000 21.56 ATOM 1333 O LEU A 200 76.691 16.873 42.026 1.000 24.91 ATOM 1334 N PHE A 201 77.391 14.922 41.160 1.000 18.56 ATOM 1335 CA PHE A 201 76.258 14.175 41.696 1.000 22.51 ATOM 1336 CB PHE A 201 75.324 13.676 40.585 1.000 18.39 ATOM 1337 CG PHE A 201 74.333 14.750 40.151 1.000 22.13 ATOM 1338 CD1 PHE A 201 74.766 15.884 39.486 1.000 21.16 ATOM 1339 CD2 PHE A 201 72.985 14.614 40.415 1.000 21.94 ATOM 1340 CE1 PHE A 201 73.870 16.865 39.098 1.000 20.75 ATOM 1341 CE2 PHE A 201 72.083 15.594 40.036 1.000 22.20 ATOM 1342 CZ PHE A 201 72.523 16.726 39.375 1.000 18.43 ATOM 1343 C PHE A 201 76.711 12.983 42.543 1.000 24.36 ATOM 1344 O PHE A 201 77.745 13.372 42.294 1.000 23.72 ATOM 1345 N GLY A 202 75.903 12.676 43.555 1.000 26.29 ATOM 1346 CA GLY A 202 76.191 11.573 44.455 1.000 27.80 ATOM 1347 C GLY A 202 75.787 10.233 43.872 1.000 26.77 ATOM 1348 O GLY A 202 74.706 9.721 44.164 1.000 32.55 ATOM 1349 N THR A 203 76.647 9.654 43.043 1.000 25.13 ATOM 1350 CA THR A 203 76.404 8.380 42.392 1.000 25.12 ATOM 1351 CB THR A 203 76.257 8.557 40.862 1.000 28.49 ATOM 1352 OG1 THR A 203 77.560 8.874 40.347 1.000 23.32 ATOM 1353 CG2 THR A 203 75.287 9.679 40.553 1.000 27.37 ATOM 1354 C THR A 203 77.565 7.429 42.650 1.000 27.93 ATOM 1355 O THR A 203 78.614 7.903 43.107 1.000 25.79 ATOM 1356 N PRO A 204 77.425 6.138 42.369 1.000 27.07 ATOM 1357 CD PRO A 204 76.190 5.445 41.943 1.000 29.16 ATOM 1358 CA PRO A 204 78.546 5.201 42.502 1.000 29.50 ATOM 1359 CB PRO A 204 77.974 3.880 41.969 1.000 27.25 ATOM 1360 CG PRO A 204 76.505 3.996 42.214 1.000 27.48 ATOM 1361 C PRO A 204 79.773 5.592 41.687 1.000 25.78 ATOM 1362 O PRO A 204 80.857 5.062 41.939 1.000 32.08 ATOM 1363 N LEU A 205 79.645 6.483 40.716 1.000 37.07 ATOM 1364 CA LEU A 205 80.788 6.983 39.963 1.000 31.42 ATOM 1365 CB LEU A 205 80.346 8.062 38.969 1.000 28.18 ATOM 1366 CG LEU A 205 81.354 8.485 37.900 1.000 35.16 ATOM 1367 CD1 LEU A 205 81.596 7.353 36.911 1.000 31.93 ATOM 1368 CD2 LEU A 205 80.884 9.746 37.187 1.000 31.91 ATOM 1369 C LEU A 205 81.856 7.554 40.889 1.000 27.98 ATOM 1370 O LEU A 205 83.042 7.313 40.676 1.000 34.06 ATOM 1371 N LEU A 206 81.465 8.320 41.904 1.000 21.36 ATOM 1372 CA LEU A 206 82.421 9.023 42.750 1.000 18.23 ATOM 1373 CB LEU A 206 81.777 10.282 43.351 1.000 19.00 ATOM 1374 CG LEU A 206 81.166 11.282 42.373 1.000 29.73 ATOM 1375 CD1 LEU A 206 80.600 12.484 43.114 1.000 26.59 ATOM 1376 CD2 LEU A 206 82.196 11.722 41.344 1.000 45.64 ATOM 1377 C LEU A 206 82.959 8.185 43.903 1.000 25.48 ATOM 1378 O LEU A 206 83.768 8.675 44.699 1.000 29.01 ATOM 1379 N THR A 207 82.518 6.943 44.017 1.000 27.24 ATOM 1380 CA THR A 207 82.834 6.112 45.176 1.000 24.16 ATOM 1381 CB THR A 207 82.002 4.814 45.180 1.000 31.81 ATOM 1382 OG1 THR A 207 80.604 5.121 45.103 1.000 33.01 ATOM 1383 CG2 THR A 207 82.189 4.062 46.492 1.000 39.64 ATOM 1384 C THR A 207 84.317 5.774 45.241 1.000 27.40 ATOM 1385 O THR A 207 84.893 5.719 46.330 1.000 34.76 ATOM 1386 N SER A 208 84.932 5.557 44.085 1.000 31.07 ATOM 1387 CA SER A 208 86.362 5.291 44.002 1.000 37.59 ATOM 1388 CB SER A 208 86.794 5.170 42.536 1.000 40.21 ATOM 1389 OG SER A 208 85.664 4.850 41.732 1.000 64.46 ATOM 1390 C SER A 208 87.164 6.379 44.711 1.000 39.66 ATOM 1391 O SER A 208 88.177 6.088 45.351 1.000 59.11 ATOM 1392 N LEU A 209 86.710 7.622 44.608 1.000 28.44 ATOM 1393 CA LEU A 209 87.362 8.752 45.254 1.000 35.84 ATOM 1394 CB LEU A 209 86.632 10.056 44.879 1.000 36.73 ATOM 1395 CG LEU A 209 86.694 10.394 43.380 1.000 35.96 ATOM 1396 CD1 LEU A 209 85.999 11.711 43.072 1.000 20.66 ATOM 1397 CD2 LEU A 209 88.146 10.411 42.921 1.000 33.37 ATOM 1398 C LEU A 209 87.414 8.605 46.770 1.000 34.49 ATOM 1399 O LEU A 209 86.475 8.101 47.383 1.000 32.58 ATOM 1400 N PRO A 210 88.512 9.043 47.374 1.000 29.27 ATOM 1401 CD PRO A 210 89.765 9.458 46.720 1.000 27.98 ATOM 1402 CA PRO A 210 88.602 9.147 48.831 1.000 29.98 ATOM 1403 CB PRO A 210 89.947 9.846 49.069 1.000 27.49 ATOM 1404 CG PRO A 210 90.746 9.460 47.866 1.000 25.08 ATOM 1405 C PRO A 210 87.479 10.015 49.389 1.000 31.11 ATOM 1406 O PRO A 210 87.131 11.047 48.810 1.000 31.99 ATOM 1407 N GLU A 211 86.929 9.576 50.514 1.000 27.60 ATOM 1408 CA GLU A 211 85.816 10.265 51.145 1.000 26.18 ATOM 1409 CB GLU A 211 85.562 9.614 52.509 1.000 40.32 ATOM 1410 CG GLU A 211 84.354 9.696 52.509 1.000 43.94 ATOM 1411 CD GLU A 211 84.054 8.131 53.884 1.000 42.42 ATOM 1412 OE1 GLU A 211 83.181 8.700 54.573 1.000 30.45 ATOM 1413 OE2 GLU A 211 84.705 7.119 54.222 1.000 31.95 ATOM 1414 C GLU A 211 86.092 11.748 51.308 1.000 24.00 ATOM 1415 O GLU A 211 85.265 12.615 51.031 1.000 24.47 ATOM 1416 N LYS A 212 87.308 12.033 21.770 1.000 22.33 ATOM 1417 CA LYS A 212 87.768 13.405 51.947 1.000 29.30 ATOM 1418 CB LYS A 212 89.228 13.403 52.387 1.000 40.01 ATOM 1419 C LYS A 212 87.595 14.237 50.680 1.000 23.78 ATOM 1420 O LYS A 212 87.161 15.389 50.730 1.000 24.76 ATOM 1421 N VAL A 213 87.925 13.677 49.521 1.000 24.58 ATOM 1422 CA VAL A 213 87.769 14.435 48.278 1.000 26.36 ATOM 1423 CB VAL A 213 88.451 13.686 47.120 1.000 35.53 ATOM 1424 CG1 VAL A 213 88.325 14.449 45.808 1.000 27.07 ATOM 1425 CG2 VAL A 213 89.916 13.443 47.469 1.000 38.54 ATOM 1426 C VAL A 213 86.297 14.679 47.965 1.000 24.27 ATOM 1427 O VAL A 213 85.865 15.790 47.657 1.000 23.99 ATOM 1428 N ARG A 214 85.503 13.619 48.050 1.000 23.64 ATOM 1429 CA ARG A 214 84.062 13.735 47.858 1.000 23.89 ATOM 1430 CB ARG A 214 83.387 12.395 48.152 1.000 28.02 ATOM 1431 CG ARG A 214 83.291 11.484 46.938 1.000 31.88 ATOM 1432 CD ARG A 214 86.728 10.064 47.279 1.000 35.66 ATOM 1433 NE ARG A 214 82.744 9.415 48.130 1.000 37.47 ATOM 1434 CZ ARG A 214 82.895 8.303 48.828 1.000 44.73 ATOM 1435 NH1 ARG A 214 84.031 7.613 48.828 1.000 37.28 ATOM 1436 NH2 ARG A 214 81.860 7.878 49.548 1.000 67.12 ATOM 1437 C ARG A 214 83.477 14.826 48.743 1.000 30.95 ATOM 1438 O ARG A 214 82.709 15.670 48.281 1.000 33.19 ATOM 1439 N ASN A 215 83.837 14.840 50.028 1.000 28.66 ATOM 1440 CA ASN A 215 83.308 15.887 50.902 1.000 27.53 ATOM 1441 CB ASN A 215 83.684 15.663 52.369 1.000 32.68 ATOM 1442 CG ASN A 215 83.258 14.304 52.883 1.000 31.08 ATOM 1443 OD1 ASN A 215 82.446 13.619 52.262 1.000 37.63 ATOM 1444 ND2 ASN A 215 86.810 13.898 54.017 1.000 43.42 ATOM 1445 C ASN A 215 83.810 17.258 50.469 1.000 18.44 ATOM 1446 O ASN A 215 83.057 18.231 50.485 1.000 30.03 ATOM 1447 N PHE A 216 85.081 17.340 50.084 1.000 22.51 ATOM 1448 CA PHE A 216 85.609 18.441 49.675 1.000 25.01 ATOM 1449 CB PHE A 216 87.113 18.554 49.401 1.000 26.17 ATOM 1450 CG PHE A 216 87.636 19.848 48.788 1.000 30.92 ATOM 1451 CD1 PHE A 216 87.820 20.969 49.576 1.000 26.31 ATOM 1452 CD2 PHE A 216 87.929 19.922 47.439 1.000 38.31 ATOM 1453 CE1 PHE A 216 88.284 22.150 49.036 1.000 28.91 ATOM 1454 CE2 PHE A 216 88.397 21.102 46.888 1.000 42.22 ATOM 1455 CZ PHE A 216 88.574 22.216 47.685 1.000 36.56 ATOM 1456 C PHE A 216 84.876 19.173 48.442 1.000 31.65 ATOM 1457 O PHE A 216 84.487 20.342 48.442 1.000 27.79 ATOM 1458 N LEU A 217 84.688 18.320 47.439 1.000 31.39 ATOM 1459 CA LEU A 217 83.933 18.685 46.238 1.000 32.23 ATOM 1460 CB LEU A 217 83.887 17.516 45.255 1.000 32.50 ATOM 1461 CG LEU A 217 85.207 16.990 44.682 1.000 29.24 ATOM 1462 CD1 LEU A 217 84.907 15.797 43.765 1.000 17.82 ATOM 1463 CD2 LEU A 217 85.962 18.082 43.943 1.000 29.21 ATOM 1464 C LEU A 217 82.524 19.136 46.611 1.000 31.73 ATOM 1465 O LEU A 217 81.996 20.132 46.107 1.000 23.72 ATOM 1466 N ALA A 218 81.886 18.401 47.526 1.000 29.13 ATOM 1467 CA ALA A 218 80.555 18.785 47.981 1.000 28.01 ATOM 1468 CB ALA A 218 80.007 17.826 49.035 1.000 24.11 ATOM 1469 C ALA A 218 80.565 20.188 48.568 1.000 24.33 ATOM 1470 O ALA A 218 79.656 20.984 48.355 1.000 24.23 ATOM 1471 N SER A 219 81.616 20.490 49.328 1.000 25.40 ATOM 1472 CA SER A 219 81.633 21.782 50.012 1.000 26.17 ATOM 1473 CB SER A 219 82.801 21.841 51.007 1.000 23.46 ATOM 1474 OG SER A 219 84.035 21.883 50.304 1.000 28.86 ATOM 1475 C SER A 219 81.731 22.929 49.026 1.000 28.77 ATOM 1476 O SER A 219 81.470 24.075 49.387 1.000 29.20 ATOM 1477 N GLN A 220 82.102 22.651 47.777 1.000 31.06 ATOM 1478 CA GLN A 220 82.336 23.755 46.850 1.000 28.95 ATOM 1479 CB GLN A 220 83.511 23.370 45.940 1.000 35.57 ATOM 1480 CG GLN A 220 84.805 23.152 46.713 1.000 46.25 ATOM 1481 CD GLN A 220 85.559 24.459 46.910 1.000 54.85 ATOM 1482 OE1 GLN A 220 85.311 25.169 47.883 1.000 67.11 ATOM 1483 NE2 GLN A 220 86.465 27.766 45.989 1.000 58.88 ATOM 1484 C GLN A 220 81.139 24.144 46.005 1.000 27.97 ATOM 1485 O GLN A 220 81.188 25.140 45.266 1.000 25.50 ATOM 1486 N VAL A 221 80.038 23.397 46.066 1.000 24.23 ATOM 1487 CA VAL A 221 78.877 23.801 45.257 1.000 19.71 ATOM 1488 CB VAL A 221 77.881 22.645 45.135 1.000 20.16 ATOM 1489 CG1 VAL A 221 76.729 23.008 44.204 1.000 16.09 ATOM 1490 CG2 VAL A 221 78.595 21.382 44.657 1.000 17.00 ATOM 1491 C VAL A 221 78.226 25.016 45.896 1.000 24.47 ATOM 1492 O VAL A 221 77.763 24.933 47.041 1.000 25.19 ATOM 1493 N PRO A 222 78.187 26.160 45.232 1.000 25.80 ATOM 1494 CD PRO A 222 78.681 26.411 43.859 1.000 24.80 ATOM 1495 CA PRO A 222 77.651 27.382 45.848 1.000 22.49 ATOM 1496 CB PRO A 222 77.602 28.367 44.666 1.000 18.73 ATOM 1497 CG PRO A 222 78.785 27.924 43.841 1.000 22.15 ATOM 1498 C PRO A 222 76.272 27.231 46.462 1.000 27.78 ATOM 1499 O PRO A 222 76.075 27.491 47.650 1.000 24.62 ATOM 1500 N PHE A 223 75.253 29.829 45.714 1.000 24.56 ATOM 1501 CA PHE A 223 73.945 26.652 46.334 1.000 20.97 ATOM 1502 CB PHE A 223 73.215 27.947 46.693 1.000 20.13 ATOM 1503 CG PHE A 223 71.883 27.618 47.370 1.000 25.97 ATOM 1504 CD1 PHE A 223 71.850 27.192 48.687 1.000 28.70 ATOM 1505 CD2 PHE A 223 70.668 27.728 46.689 1.000 22.64 ATOM 1506 CE1 PHE A 223 70.654 26.880 49.320 1.000 25.50 ATOM 1507 CE2 PHE A 223 69.488 27.424 47.313 1.000 25.33 ATOM 1508 CZ PHE A 223 69.464 26.993 48.629 1.000 22.68 ATOM 1509 C PHE A 223 73.057 25.813 45.415 1.000 26.48 ATOM 1510 O PHE A 223 72.918 26.178 44.248 1.000 24.24 ATOM 1511 N PRO A 224 72.466 24.733 45.911 1.000 28.80 ATOM 1512 CD PRO A 224 71.556 23.870 45.133 1.000 28.23 ATOM 1513 CA PRO A 224 72.625 24.268 47.290 1.000 29.22 ATOM 1514 CB PRO A 224 71.509 23.232 47.436 1.000 31.63 ATOM 1515 CG PRO A 224 71.279 22.721 46.058 1.000 29.47 ATOM 1516 C PRO A 224 73.982 23.602 47.531 1.000 28.36 ATOM 1517 O PRO A 224 74.550 22.999 46.621 1.000 22.58 ATOM 1518 N SER A 225 74.484 23.778 48.751 1.000 25.87 ATOM 1519 CA SER A 225 75.832 23.351 49.090 1.000 29.25 ATOM 1520 CB SER A 225 76.367 24.152 50.283 1.000 37.81 ATOM 1521 OG SER A 225 76.577 25.493 49.874 1.000 56.13 ATOM 1522 C SER A 225 75.883 21.863 49.385 1.000 29.47 ATOM 1523 O SER A 225 75.952 21.398 50.516 1.000 28.64 ATOM 1524 N ARG A 226 75.850 21.105 48.293 1.000 23.34 ATOM 1525 CA ARG A 226 75.876 19.658 48.378 1.000 21.20 ATOM 1526 CB ARG A 226 74.594 19.134 49.026 1.000 20.65 ATOM 1527 CG ARG A 226 73.340 19.637 48.306 1.000 20.10 ATOM 1528 CD ARG A 226 72.203 18.633 48.397 1.000 23.97 ATOM 1529 NE ARG A 226 70.932 19.239 47.978 1.000 23.27 ATOM 1530 CZ ARG A 226 70.369 19.014 46.796 1.000 27.29 ATOM 1531 NH1 ARG A 226 69.219 19.600 46.488 1.000 20.66 ATOM 1532 NH2 ARG A 226 70.943 18.206 45.908 1.000 22.51 ATOM 1533 C ARG A 226 76.007 19.003 46.972 1.000 24.78 ATOM 1534 O ARG A 226 75.759 19.779 45.986 1.000 24.98 ATOM 1535 N LEU A 227 76.368 17.812 46.899 1.000 21.08 ATOM 1536 CA LEU A 227 76.314 17.125 45.617 1.000 25.85 ATOM 1537 CB LEU A 227 76.849 15.701 45.778 1.000 25.37 ATOM 1538 CG LEU A 227 78.246 15.581 46.398 1.000 24.53 ATOM 1539 CD1 LEU A 227 78.615 14.112 46.539 1.000 23.43 ATOM 1540 CD2 LEU A 227 79.254 16.352 45.562 1.000 19.26 ATOM 1541 C LEU A 227 74.885 17.114 45.105 1.000 25.75 ATOM 1542 O LEU A 227 73.932 17.166 45.890 1.000 21.27 ATOM 1543 N GLY A 228 74.697 17.041 43.786 1.000 23.15 ATOM 1544 CA GLY A 228 73.327 16.959 43.294 1.000 19.97 ATOM 1545 C GLY A 228 72.747 15.590 43.606 1.000 21.85 ATOM 1546 O GLY A 228 73.477 14.604 43.695 1.000 22.71 ATOM 1547 N ASP A 229 71.423 15.532 43.766 1.000 23.70 ATOM 1548 CA ASP A 229 70.781 14.228 43.962 1.000 21.75 ATOM 1549 CB ASP A 229 69.594 14.376 44.909 1.000 25.58 ATOM 1550 CG ASP A 229 69.011 13.036 45.317 1.000 37.77 ATOM 1551 OD1 ASP A 229 68.989 12.691 46.522 1.000 52.48 ATOM 1552 OD2 ASP A 229 68.565 12.322 44.393 1.000 37.02 ATOM 1553 C ASP A 229 70.362 13.661 42.618 1.000 18.38 ATOM 1554 O ASP A 229 69.795 14.402 41.817 1.000 21.95 ATOM 1555 N PRO A 230 70.630 12.396 42.353 1.000 24.18 ATOM 1556 CD PRO A 230 71.242 11.395 43.258 1.000 23.15 ATOM 1557 CA PRO A 230 70.332 11.833 41.027 1.000 23.50 ATOM 1558 CB PRO A 230 70.618 10.340 41.234 1.000 24.52 ATOM 1559 CG PRO A 230 71.705 10.352 42.273 1.000 23.78 ATOM 1560 C PRO A 230 68.895 12.054 40.589 1.000 26.53 ATOM 1561 O PRO A 230 68.602 12.084 39.387 1.000 25.38 ATOM 1562 N ALA A 231 67.961 12.207 41.528 1.000 26.35 ATOM 1563 CA ALA A 231 66.579 12.467 41.116 1.000 26.18 ATOM 1564 CB ALA A 231 65.608 12.325 42.280 1.000 21.25 ATOM 1565 C ALA A 231 66.449 13.855 40.495 1.000 26.64 ATOM 1566 O ALA A 231 65.546 14.075 39.478 1.000 26.06 ATOM 1567 N GLU A 232 67.322 14.786 40.857 1.000 22.42 ATOM 1568 CA GLU A 232 67.304 16.120 40.250 1.000 23.24 ATOM 1569 CB GLU A 232 68.224 17.072 41.030 1.000 23.89 ATOM 1570 CG GLU A 232 67.618 17.531 42.345 1.000 22.94 ATOM 1571 CD GLU A 232 68.572 18.110 43.357 1.000 22.44 ATOM 1572 OE1 GLU A 232 69.783 17.800 43.363 1.000 22.54 ATOM 1573 OE2 GLU A 232 68.106 18.906 44.206 1.000 22.99 ATOM 1574 C GLU A 232 67.677 16.041 38.772 1.000 21.16 ATOM 1575 O GLU A 232 67.133 16.772 37.943 1.000 23.00 ATOM 1576 N TYR A 233 68.600 15.162 37.418 1.000 18.83 ATOM 1577 CA TYR A 233 68.921 14.913 37.015 1.000 21.13 ATOM 1578 CB TYR A 233 70.096 13.937 36.893 1.000 19.96 ATOM 1579 CG TYR A 233 70.437 13.521 35.475 1.000 21.89 ATOM 1580 CD1 TYR A 233 71.301 14.274 34.688 1.000 19.55 ATOM 1581 CE1 TYR A 233 71.606 13.877 33.393 1.000 18.37 ATOM 1582 CD2 TYR A 233 69.307 12.366 34.909 1.000 19.47 ATOM 1583 CE2 TYR A 233 70.197 11.970 33.624 1.000 22.32 ATOM 1584 CZ TYR A 233 71.056 12.740 32.864 1.000 21.80 ATOM 1585 OH TYR A 233 71.345 12.329 31.579 1.000 22.58 ATOM 1586 C TYR A 233 67.693 14.366 36.285 1.000 27.74 ATOM 1587 O TYR A 233 67.365 14.803 35.181 1.000 27.25 ATOM 1588 N ALA A 234 67.043 13.382 36.903 1.000 23.68 ATOM 1589 CA ALA A 234 65.851 12.738 36.377 1.000 20.29 ATOM 1590 CB ALA A 234 62.349 11.677 37.349 1.000 23.40 ATOM 1591 C ALA A 234 64.740 13.744 36.094 1.000 20.45 ATOM 1592 O ALA A 234 64.060 13.659 35.066 1.000 25.13 ATOM 1593 N HIS A 235 64.545 14.693 37.004 1.000 19.46 ATOM 1594 CA HIS A 235 63.560 15.746 36.801 1.000 20.05 ATOM 1595 CB HIS A 235 63.490 16.680 38.008 1.000 20.64 ATOM 1596 CG HIS A 235 62.661 17.910 37.798 1.000 23.05 ATOM 1597 CD2 HIS A 235 62.979 19.150 37.361 1.000 21.17 ATOM 1598 ND1 HIS A 235 61.306 17.954 38.072 1.000 28.32 ATOM 1599 CE1 HIS A 235 60.826 19.155 37.806 1.000 22.48 ATOM 1600 NE2 HIS A 235 61.825 19.898 37.370 1.000 27.72 ATOM 1601 C HIS A 235 63.890 16.550 35.549 1.000 24.63 ATOM 1602 O HIS A 235 62.975 16.892 37.798 1.000 24.01 ATOM 1603 N LEU A 236 65.167 16.867 35.324 1.000 24.45 ATOM 1604 CA LEU A 236 65.509 17.681 34.160 1.000 22.07 ATOM 1605 CB LEU A 236 66.950 18.181 34.211 1.000 20.78 ATOM 1606 CG LEU A 236 67.404 19.047 33.026 1.000 18.62 ATOM 1607 CD1 LEU A 236 66.248 20.196 32.799 1.000 16.03 ATOM 1608 CD2 LEU A 236 68.809 19.579 33.252 1.000 16.04 ATOM 1609 C LEU A 236 65.266 16.903 32.866 1.000 21.70 ATOM 1610 O LEU A 236 64.772 17.483 31.900 1.000 20.42 ATOM 1611 N VAL A 237 65.582 15.617 32.841 1.000 21.20 ATOM 1612 CA VAL A 237 65.283 14.783 31.675 1.000 21.16 ATOM 1613 CB VAL A 237 65.172 13.318 31.863 1.000 23.98 ATOM 1614 CG1 VAL A 237 65.154 12.454 30.730 1.000 23.53 ATOM 1615 CG2 VAL A 237 67.225 13.178 31.928 1.000 21.01 ATOM 1616 C VAL A 237 63.789 14.818 31.361 1.000 24.81 ATOM 1617 O VAL A 237 63.371 14.951 30.208 1.000 23.68 ATOM 1618 N GLN A 238 62.942 14.701 32.383 1.000 22.85 ATOM 1619 CA GLN A 238 61.503 14.737 32.105 1.000 23.14 ATOM 1620 CB GLN A 238 60.680 14.420 33.355 1.000 27.65 ATOM 1621 CG GLN A 238 59.175 14.510 33.117 1.000 34.44 ATOM 1622 CD GLN A 238 58.382 14.022 34.313 1.000 45.36 ATOM 1623 OE1 GLN A 238 58.910 13.369 35.216 1.000 44.78 ATOM 1624 NE2 GLN A 238 57.091 14.335 34.341 1.000 41.18 ATOM 1625 C GLN A 238 61.074 16.092 31.546 1.000 20.15 ATOM 1626 O GLN A 238 60.265 16.158 30.626 1.000 28.26 ATOM 1627 N ALA A 239 31.625 17.165 32.104 1.000 16.27 ATOM 1628 CA ALA A 239 61.311 18.514 31.669 1.000 17.56 ATOM 1629 CB ALA A 239 62.049 19.520 32.536 1.000 21.61 ATOM 1630 C ALA A 239 61.664 18.722 30.198 1.000 22.67 ATOM 1631 O ALA A 239 60.942 19.377 29.457 1.000 23.10 ATOM 1632 N ILE A 240 62.790 18.165 29.781 1.000 20.80 ATOM 1633 CA ILE A 240 63.216 18.205 28.386 1.000 25.50 ATOM 1634 CB ILE A 240 64.683 17.734 28.278 1.000 23.55 ATOM 1635 CG2 ILE A 240 65.037 17.338 26.860 1.000 20.26 ATOM 1636 CG1 ILE A 240 62.683 18.769 28.827 1.000 17.72 ATOM 1637 CD1 ILE A 240 67.703 18.186 28.998 1.000 19.57 ATOM 1638 C ILE A 240 62.314 17.348 27.511 1.000 26.46 ATOM 1639 O ILE A 240 62.916 17.735 26.411 1.000 21.98 ATOM 1640 N ILE A 241 61.969 16.155 27.992 1.000 21.35 ATOM 1641 CA ILE A 241 61.046 15.306 27.238 1.000 26.98 ATOM 1642 CB ILE A 241 60.734 13.972 27.940 1.000 27.84 ATOM 1643 CG2 ILE A 241 59.573 13.265 27.244 1.000 23.88 ATOM 1644 CG1 ILE A 241 61.926 13.023 28.066 1.000 22.84 ATOM 1645 CD1 ILE A 241 61.693 11.863 29.011 1.000 20.80 ATOM 1646 C ILE A 241 59.739 16.056 26.990 1.000 27.61 ATOM 1647 O ILE A 241 59.144 16.033 25.913 1.000 24.04 ATOM 1648 N GLU A 242 29.286 16.746 28.036 1.000 21.41 ATOM 1649 CA GLU A 242 57.969 17.364 27.977 1.000 23.08 ATOM 1650 CB GLU A 242 57.499 17.647 29.408 1.000 22.57 ATOM 1651 CG GLU A 242 57.170 16.396 30.206 1.000 25.70 ATOM 1652 CD GLU A 242 56.396 16.747 31.475 1.000 31.32 ATOM 1653 OE1 GLU A 242 55.646 15.891 31.987 1.000 41.56 ATOM 1654 OE2 GLU A 242 56.553 17.892 31.951 1.000 38.20 ATOM 1655 C GLU A 242 57.936 18.649 27.170 1.000 27.56 ATOM 1656 O GLU A 242 56.914 18.945 26.552 1.000 27.92 ATOM 1657 N ASN A 243 59.015 19.426 27.170 1.000 22.75 ATOM 1658 CA ASN A 243 59.011 20.717 26.485 1.000 24.21 ATOM 1659 CB ASN A 243 59.999 21.671 27.156 1.000 21.86 ATOM 1660 CG ASN A 243 59.811 23.108 26.172 1.000 23.53 ATOM 1661 OD1 ASN A 243 89.775 23.431 25.522 1.000 22.67 ATOM 1662 ND2 ASN A 243 59.700 23.988 27.689 1.000 19.20 ATOM 1663 C ASN A 243 59.356 20.565 25.009 1.000 27.29 ATOM 1664 O ASN A 243 60.489 20.231 24.654 1.000 24.50 ATOM 1665 N PRO A 244 58.382 20.804 21.138 1.000 27.24 ATOM 1666 CD PRO A 244 57.005 21.238 24.434 1.000 24.08 ATOM 1667 CA PRO A 244 58.603 20.626 22.700 1.000 22.73 ATOM 1668 CB PRO A 244 57.222 20.911 22.084 1.000 23.36 ATOM 1669 CG PRO A 244 56.269 20.716 23.222 1.000 26.47 ATOM 1670 C PRO A 244 59.603 21.596 22.100 1.000 21.55 ATOM 1671 O PRO A 244 60.085 21.321 20.988 1.000 24.58 ATOM 1672 N PHE A 245 59.941 22.717 22.735 1.000 21.03 ATOM 1673 CA PHE A 245 60.793 23.659 21.993 1.000 19.57 ATOM 1674 CB PHE A 245 60.283 25.086 22.178 1.000 22.58 ATOM 1675 CG PHE A 245 60.458 26.021 20.995 1.000 18.83 ATOM 1676 CD1 PHE A 245 61.118 27.224 21.130 1.000 17.04 ATOM 1677 CD2 PHE A 245 59.957 25.695 19.742 1.000 18.90 ATOM 1678 CE1 PHE A 245 61.281 28.103 20.068 1.000 19.82 ATOM 1679 CE2 PHE A 245 60.103 26.548 18.663 1.000 16.29 ATOM 1680 CZ PHE A 245 60.797 27.749 18.832 1.000 18.24 ATOM 1681 C PHE A 245 62.263 23.549 22.388 1.000 25.70 ATOM 1682 O PHE A 245 63.087 24.304 21.873 1.000 19.98 ATOM 1683 N LEU A 246 62.630 22.635 23.279 1.000 23.56 ATOM 1684 CA LEU A 246 64.026 22.477 23.685 1.000 22.39 ATOM 1685 CB LEU A 246 64.141 21.902 25.102 1.000 21.56 ATOM 1686 CG LEU A 246 63.840 22.873 26.249 1.000 23.45 ATOM 1687 CD1 LEU A 246 63.735 22.128 27.570 1.000 23.33 ATOM 1688 CD2 LEU A 246 64.900 23.962 26.334 1.000 20.46 ATOM 1689 C LEU A 246 64.782 21.575 22.715 1.000 20.66 ATOM 1690 O LEU A 246 64.517 20.378 22.630 1.000 21.20 ATOM 1691 N ASN A 247 65.735 22.145 21.985 1.000 20.82 ATOM 1692 CA ASN A 247 66.483 21.349 21.010 1.000 21.25 ATOM 1693 CB ASN A 247 65.671 21.292 19.718 1.000 21.44 ATOM 1694 CG ASN A 247 66.084 20.187 18.770 1.000 27.16 ATOM 1695 OD1 ASN A 247 66.899 19.328 19.096 1.000 20.56 ATOM 1696 ND2 ASN A 247 65.498 20.210 17.569 1.000 22.46 ATOM 1697 C ASN A 247 67.862 21.932 20.741 1.000 19.13 ATOM 1698 O ASN A 247 68.019 23.151 20.747 1.000 18.86 ATOM 1699 N GLY A 248 68.861 21.095 20.493 1.000 19.82 ATOM 1700 CA GLY A 248 70.191 21.529 20.123 1.000 20.18 ATOM 1701 C GLY A 248 70.947 22.319 21.161 1.000 21.65 ATOM 1702 O GLY A 248 71.837 23.111 20.846 1.000 18.31 ATOM 1703 N GLU A 249 70.617 22.123 22.436 1.000 19.76 ATOM 1704 CA GLU A 249 71.193 22.933 23.512 1.000 15.34 ATOM 1705 CB GLU A 249 70.093 23.812 24.096 1.000 17.49 ATOM 1706 CG GLU A 249 70.339 24.393 25.479 1.000 18.34 ATOM 1707 CD GLU A 249 71.417 25.457 25.495 1.000 20.71 ATOM 1708 OE1 GLU A 249 71.291 26.430 26.270 1.000 24.53 ATOM 1709 OE2 GLU A 249 72.399 25.321 24.737 1.000 20.71 ATOM 1710 C GLU A 249 71.827 22.049 24.576 1.000 20.26 ATOM 1711 O GLU A 249 71.485 20.874 24.713 1.000 18.20 ATOM 1712 N VAL A 250 72.758 22.628 25.324 1.000 20.14 ATOM 1713 CA VAL A 250 73.423 21.963 26.444 1.000 15.45 ATOM 1714 CB VAL A 250 74.950 21.971 26.285 1.000 23.58 ATOM 1715 CG1 VAL A 250 75.633 21.356 27.501 1.000 21.33 ATOM 1716 CG2 VAL A 250 75.346 21.233 25.011 1.000 20.50 ATOM 1717 C VAL A 250 73.029 22.660 27.744 1.000 19.05 ATOM 1718 O VAL A 250 73.131 23.892 27.823 1.000 18.90 ATOM 1719 N ILE A 251 72.577 21.905 28.746 1.000 17.48 ATOM 1720 CA ILE A 251 72.115 22.552 29.977 1.000 19.87 ATOM 1721 CB ILE A 251 70.639 22.211 30.259 1.000 19.82 ATOM 1722 CG2 ILE A 251 70.190 22.867 31.567 1.000 18.96 ATOM 1723 CG1 ILE A 251 69.670 22.552 29.127 1.000 16.79 ATOM 1724 CD1 ILE A 251 68.244 22.113 29.385 1.000 18.75 ATOM 1725 C ILE A 251 72.953 22.143 31.183 1.000 18.61 ATOM 1726 O ILE A 251 73.009 20.947 31.501 1.000 20.95 ATOM 1727 N ARG A 252 73.594 23.118 31.822 1.000 20.09 ATOM 1728 CA ARG A 252 74.390 22.869 33.018 1.000 20.43 ATOM 1729 CB ARG A 252 76.386 24.034 33.378 1.000 20.29 ATOM 1730 CG ARG A 252 76.386 24.442 32.411 1.000 22.69 ATOM 1731 CD ARG A 252 77.182 25.646 32.914 1.000 21.00 ATOM 1732 NE ARG A 252 77.981 25.296 34.708 1.000 19.89 ATOM 1733 CZ ARG A 252 79.304 25.251 34.157 1.000 21.01 ATOM 1734 NH1 ARG A 252 79.896 24.909 35.293 1.000 16.77 ATOM 1735 NH2 ARG A 252 80.069 25.543 33.114 1.000 20.53 ATOM 1736 C ARG A 252 73.453 22.609 34.008 1.000 19.55 ATOM 1737 O ARG A 252 72.587 23.437 34.488 1.000 15.60 ATOM 1738 N LEU A 253 73.623 21.494 34.897 1.000 19.36 ATOM 1739 CA LEU A 253 72.859 21.189 36.109 1.000 18.74 ATOM 1740 CB LEU A 253 71.984 19.960 35.898 1.000 17.63 ATOM 1741 CG LEU A 253 71.116 19.524 37.089 1.000 20.75 ATOM 1742 CD1 LEU A 253 70.028 20.566 37.333 1.000 14.44 ATOM 1743 CD2 LEU A 253 70.514 18.148 36.872 1.000 14.92 ATOM 1744 C LEU A 253 73.854 20.999 37.247 1.000 21.59 ATOM 1745 O LEU A 253 74.367 19.906 37.465 1.000 19.92 ATOM 1746 N ASP A 254 74.167 22.074 38.791 1.000 19.66 ATOM 1747 CA ASP A 254 75.366 22.050 38.791 1.000 19.66 ATOM 1748 CB ASP A 254 76.544 22.469 37.883 1.000 15.11 ATOM 1749 CG ASP A 254 76.311 23.832 37.262 1.000 21.56 ATOM 1750 OD1 ASP A 254 75.534 24.535 37.673 1.000 18.87 ATOM 1751 OD2 ASP A 254 77.085 24.205 35.351 1.000 22.35 ATOM 1752 C ASP A 254 75.369 22.971 39.994 1.000 20.87 ATOM 1753 O ASP A 254 76.442 23.142 40.582 1.000 23.02 ATOM 1754 N GLY A 255 74.248 23.582 40.371 1.000 21.44 ATOM 1755 CA GLY A 255 74.249 24.391 41.590 1.000 17.40 ATOM 1756 C GLY A 255 75.152 25.600 41.497 1.000 24.03 ATOM 1757 O GLY A 255 75.619 26.088 42.529 1.000 20.64 ATOM 1758 N ALA A 256 75.377 26.065 40.270 1.000 23.32 ATOM 1759 CA ALA A 256 76.148 27.265 39.372 1.000 21.34 ATOM 1760 CB ALA A 256 75.654 28.440 40.814 1.000 18.73 ATOM 1761 C ALA A 256 77.646 27.063 40.179 1.000 19.93 ATOM 1762 O ALA A 256 78.420 28.029 40.229 1.000 19.19 ATOM 1763 N ILE A 257 78.106 25.815 40.309 1.000 17.99 ATOM 1764 CA ILE A 257 79.550 25.652 40.528 1.000 19.13 ATOM 1765 CB ILE A 257 79.893 24.238 41.020 1.000 18.18 ATOM 1766 CG2 ILE A 257 79.829 23.235 39.875 1.000 23.53 ATOM 1767 CG1 ILE A 257 81.250 24.126 41.723 1.000 18.23 ATOM 1768 CD1 ILE A 257 81.531 22.750 42.290 1.000 16.33 ATOM 1769 C ILE A 257 80.337 25.944 39.250 1.000 24.61 ATOM 1770 O ILE A 257 79.827 25.788 38.139 1.000 17.90 ATOM 1771 N ARG A 258 81.583 26.366 39.421 1.000 21.54 ATOM 1772 CA ARG A 258 82.544 26.437 38.321 1.000 18.05 ATOM 1773 CB ARG A 258 82.840 27.868 37.900 1.000 17.08 ATOM 1774 CG ARG A 258 81.674 28.634 37.604 1.000 18.32 ATOM 1775 CD ARG A 258 81.189 27.958 36.030 1.000 21.14 ATOM 1776 NE ARG A 258 80.078 28.673 35.403 1.000 21.78 ATOM 1777 CZ ARG A 258 78.799 28.476 35.694 1.000 22.43 ATOM 1778 NH1 ARG A 258 77.865 29.176 35.066 1.000 18.08 ATOM 1779 NH2 ARG A 258 78.461 27.578 36.615 1.000 18.74 ATOM 1780 C ARG A 258 83.813 25.725 38.774 1.000 21.78 ATOM 1781 O ARG A 258 84.418 26.130 39.766 1.000 21.81 ATOM 1782 N MET A 259 84.246 24.671 38.100 1.000 21.16 ATOM 1783 CA MET A 259 85.366 23.892 38.637 1.000 23.09 ATOM 1784 CB MET A 259 85.406 22.519 37.953 1.000 23.03 ATOM 1785 CG MET A 259 84.099 21.752 38.058 1.000 26.30 ATOM 1786 SD MET A 259 83.442 21.712 39.743 1.000 27.07 ATOM 1787 CE MET A 259 84.624 20.636 40.546 1.000 26.15 ATOM 1788 C MET A 259 86.723 24.554 38.505 1.000 29.45 ATOM 1789 O MET A 259 87.113 25.112 37.473 1.000 28.26 ATOM 1790 N GLN A 260 27.445 24.505 39.594 1.000 29.83 ATOM 1791 CA GLN A 260 88.838 24.069 39.623 1.000 25.68 ATOM 1792 CB GLN A 260 89.054 28.670 41.014 1.000 30.10 ATOM 1793 CG GLN A 260 88.941 27.172 41.032 1.000 43.43 ATOM 1794 CD GLN A 260 89.302 27.235 39.784 1.000 50.49 ATOM 1795 OE1 GLN A 260 90.325 28.634 39.755 1.000 40.10 ATOM 1796 NE2 GLN A 260 88.520 27.897 38.714 1.000 67.81 ATOM 1797 C GLN A 260 89.862 24.012 39.243 1.000 24.65 ATOM 1798 O GLN A 260 89.449 22.852 39.076 1.000 22.12 ATOM 1799 N PRO A 261 91.136 24.340 39.072 1.000 22.80 ATOM 1800 CD PRO A 261 91.766 25.666 39.162 1.000 26.19 ATOM 1801 CA PRO A 261 92.121 23.308 38.708 1.000 22.38 ATOM 1802 CB PRO A 261 93.465 24.021 35.882 1.000 23.53 ATOM 1803 CG PRO A 261 93.140 25.448 35.596 1.000 27.38 ATOM 1804 C PRO A 261 92.074 22.109 39.643 1.000 23.33 ATOM 1805 OT1 PRO A 261 92.038 22.366 40.861 1.000 26.80 ATOM 1806 OT2 PRO A 261 92.043 20.977 39.140 1.000 24.26 ATOM 1807 PN LIG A 262 79.866 8.049 36.850 1.000 21.10 ATOM 1808 O1N LIG A 262 77.161 9.214 37.816 1.000 19.63 ATOM 1809 O2N LIG A 262 78.412 7.604 36.951 1.000 20.28 ATOM 1810 O3P LIG A 262 77.863 6.917 37.203 1.000 23.34 ATOM 1811 O5M LIG A 262 77.188 8.537 35.356 1.000 26.86 ATOM 1812 C5M LIG A 262 76.146 8.614 34.334 1.000 23.59 ATOM 1813 C4M LIG A 262 76.601 9..638 33.328 1.000 23.45 ATOM 1814 O4M LIG A 262 76.662 10.947 33.848 1.000 26.65 ATOM 1815 C3M LIG A 262 78.028 9.344 32.697 1.000 24.43 ATOM 1816 O3M LIG A 262 78.068 9.688 31.290 1.000 32.36 ATOM 1817 C2M LIG A 262 78.922 10.273 33.544 1.000 19.91 ATOM 1818 O2M LIG A 262 80.125 10.601 32.794 1.000 18.63 ATOM 1819 C1M LIG A 262 77.987 11.498 33.713 1.000 19.38 ATOM 1820 N1N LIG A 262 78.345 12.467 34.776 1.000 15.56 ATOM 1821 C6N LIG A 262 78.804 13.791 34.353 1.000 11.07 ATOM 1822 C5N LIG A 262 79.102 14.736 35.267 1.000 22.79 ATOM 1823 C4N LIG A 262 79.372 14.335 36.735 1.000 20.14 ATOM 1824 C3N LIG A 262 78.582 13.044 37.131 1.000 15.94 ATOM 1825 C2N LIG A 262 78.264 12.124 36.205 1.000 19.61 ATOM 1826 C7N LIG A 262 78.486 12.780 38.627 1.000 18.21 ATOM 1827 O7N LIG A 262 78.848 13.651 39.435 1.000 24.82 ATOM 1828 N7N LIG A 262 78.006 11.610 38.987 1.000 18.62 ATOM 1829 PA LIG A 262 77.561 5.422 37.391 1.000 28.11 ATOM 1830 O1A LIG A 262 78.894 4.662 37.439 1.000 22.53 ATOM 1831 O2A LIG A 262 76.764 5.153 38.682 1.000 33.29 ATOM 1832 O5B LIG A 262 76.695 4.845 36.178 1.000 28.65 ATOM 1833 C5B LIG A 262 77.355 4.504 34.932 1.000 32.11 ATOM 1834 C4B LIG A 262 76.714 3.251 34.284 1.000 27.97 ATOM 1835 O4B LIG A 262 77.188 3.143 32.914 1.000 32.15 ATOM 1836 C3B LIG A 262 77.031 1.916 35.013 1.000 25.46 ATOM 1837 O3B LIG A 262 75.811 1.148 35.157 1.000 32.29 ATOM 1838 C2B LIG A 262 77.960 1.198 34.001 1.000 26.52 ATOM 1839 O2B LIG A 262 77.862 −0.237 34.126 1.000 31.44 ATOM 1840 C1B LIG A 262 77.427 1.738 32.649 1.000 33.69 ATOM 1841 N9A LIG A 262 78.396 1.552 31.519 1.000 27.56 ATOM 1842 C4A LIG A 262 78.161 1.003 30.254 1.000 22.23 ATOM 1843 N3A LIG A 262 76.989 0.455 29.579 1.000 25.87 ATOM 1844 C2A LIG A 262 77.176 0.033 28.351 1.000 26.73 ATOM 1845 N1A LIG A 262 78.279 0.037 27.632 1.000 27.79 ATOM 1846 C6A LIG A 262 79.396 0.518 28.154 1.000 27.44 ATOM 1847 C5A LIG A 262 79.411 1.038 29.510 1.000 22.37 ATOM 1848 N7A LIG A 262 80.444 1.588 30.265 1.000 23.23 ATOM 1849 C8A LIG A 262 79.747 1.856 31.414 1.000 20.75 ATOM 1850 N6A LIG A 262 80.554 0.221 27.558 1.000 28.05 ATOM 1851 C LIG A 262 86.532 12.596 38.895 1.000 36.33 ATOM 1852 C1 LIG A 262 87.716 13.547 38.393 1.000 43.35 ATOM 1853 N LIG A 262 88.747 13.908 39.257 1.000 45.45 ATOM 1854 O LIG A 262 87.661 13.937 37.206 1.000 50.12 ATOM 1855 C2 LIG A 262 88.763 13.383 40.662 1.000 45.14 ATOM 1856 C3 LIG A 262 88.417 14.342 41.834 1.000 39.71 ATOM 1857 C4 LIG A 262 89.819 14.827 38.761 1.000 44.30 ATOM 1858 C5 LIG A 262 89.602 16.294 39.221 1.000 48.68 ATOM 1859 C6 LIG A 262 89.419 16.470 40.739 1.000 52.16 ATOM 1860 C7 LIG A 262 88.192 15.801 41.385 1.000 48.56 ATOM 1861 C8 LIG A 262 86.919 11.070 38.927 1.000 37.05 ATOM 1862 C9 LIG A 262 86.039 10.178 39.567 1.000 40.45 ATOM 1863 C10 LIG A 262 86.308 8.812 39.624 1.000 35.05 ATOM 1864 C11 LIG A 262 87.482 8.325 39.053 1.000 33.43 ATOM 1865 C12 LIG A 262 88.359 9.191 38.406 1.000 34.29 ATOM 1866 C13 LIG A 262 88.092 10.560 38.358 1.000 32.93 ATOM 1867 C15 LIG A 262 84.992 12.198 37.018 1.000 31.80 ATOM 1868 N1 LIG A 262 83.945 12.171 6.253 1.000 35.97 ATOM 1869 C16 LIG A 262 82.786 12.926 36.676 1.000 26.22 ATOM 1870 C17 LIG A 262 82.816 13.642 37.893 1.000 27.12 ATOM 1871 C18 LIG A 262 84.093 13.620 38.766 1.000 30.03 ATOM 1872 N2 LIG A 262 85.193 12.803 38.165 1.000 35.96 ATOM 1873 S LIG A 262 84.095 14.537 40.290 1.000 29.89 ATOM 1874 C19 LIG A 262 81.624 14.284 38.089 1.000 27.34 ATOM 1875 N3 LIG A 262 80.834 13.998 36.974 1.000 26.99 ATOM 1876 N4 LIG A 262 81.533 13.152 36.151 1.000 21.47 ATOM 1877 CB SER B 7 111.935 37.270 18.577 1.000 66.13 ATOM 1878 C SER B 7 110.628 35.164 18.813 1.000 46.22 ATOM 1879 O SER B 7 110.939 34.462 19.779 1.000 51.08 ATOM 1880 N SER B 7 110.142 37.116 20.244 1.000 60.83 ATOM 1881 CA SER B 7 110.571 36.681 18.917 1.000 52.01 ATOM 1882 N VAL B 8 110.333 34.638 17.623 1.000 39.96 ATOM 1883 CA VAL B 8 110.396 33.185 17.459 1.000 36.17 ATOM 1884 CB VAL B 8 109.250 32.662 16.582 1.000 37.32 ATOM 1885 CG1 VAL B 8 107.898 33.067 17.159 1.000 31.50 ATOM 1886 CG2 VAL B 8 109.400 33.182 15.161 1.000 28.98 ATOM 1887 C VAL B 8 111.745 32.781 16.869 1.000 30.70 ATOM 1888 O VAL B 8 112.019 31.602 16.641 1.000 35.02 ATOM 1889 N LYS B 9 112.596 33.767 16.617 1.000 27.16 ATOM 1890 CA LYS B 9 113.944 33.473 16.135 1.000 30.39 ATOM 1891 CB LYS B 9 114.753 34.756 15.991 1.000 29.44 ATOM 1892 C LYS B 9 114.635 32.490 17.073 1.000 32.76 ATOM 1893 O LYS B 9 114.688 32.689 18.289 1.000 35.63 ATOM 1894 N GLY B 10 115.160 31.399 16.527 1.000 33.78 ATOM 1895 CA GLY B 10 115.891 30.436 17.329 1.000 33.33 ATOM 1896 C GLY B 10 115.042 29.382 17.990 1.000 32.26 ATOM 1897 O GLY B 10 115.570 28.369 18.453 1.000 38.86 ATOM 1898 N LEU B 11 113.729 29.580 18.047 1.000 28.07 ATOM 1899 CA LEU B 11 112.840 28.565 18.607 1.000 23.95 ATOM 1900 CB LEU B 11 111.455 29.191 18.812 1.000 26.82 ATOM 1901 CG LEU B 11 111.409 30.356 19.811 1.000 33.74 ATOM 1902 CD1 LEU B 11 110.025 30.980 19.884 1.000 39.05 ATOM 1903 CD2 LEu B 11 111.848 29.890 21.194 1.000 29.81 ATOM 1904 C LEU B 11 112.747 27.342 17.707 1.000 23.70 ATOM 1905 o LEU B 11 112.922 27.452 16.490 1.000 26.55 ATOM 1906 N VAL B 12 112.476 26.173 18.268 1.000 22.02 ATOM 1907 CA VAL B 12 112.260 24.944 17.510 1.000 24.81 ATOM 1908 CB VAL B 12 113.162 23.803 18.016 1.000 26.08 ATOM 1909 CG1 VAL B 12 112.893 22.513 17.258 1.000 24.44 ATOM 1910 CG2 VAL B 12 114.632 24.197 17.897 1.000 26.10 ATOM 1911 C VAL B 12 110.804 24.489 17.581 1.000 28.66 ATOM 1912 O VAL B 12 110.278 24.226 18.666 1.000 26.85 ATOM 1913 N ALA B 13 110.140 24.380 16.440 1.000 26.46 ATOM 1914 CA ALA B 13 108.743 23.981 16.366 1.000 26.62 ATOM 1915 CB ALA B 13 107.929 25.058 15.643 1.000 22.29 ATOM 1916 C ALA B 13 108.521 22.657 15.653 1.000 25.93 ATOM 1917 O ALA B 13 109.050 22.444 14.556 1.000 27.28 ATOM 1918 N VAL B 14 107.735 21.790 16.277 1.000 17.65 ATOM 1919 CA VAL B 14 107.277 20.556 15.655 1.000 20.86 ATOM 1920 CB VAL B 14 107.358 19.366 16.617 1.000 22.80 ATOM 1921 CG1 VAL B 14 106.621 18.133 16.114 1.000 19.92 ATOM 1922 CG2 VAL B 14 108.824 19.012 16.861 1.000 22.22 ATOM 1923 C VAL B 14 105.849 20.790 15.160 1.000 27.03 ATOM 1924 O VAL B 14 104.970 21.108 15.963 1.000 25.82 ATOM 1925 N ILE B 15 105.610 20.658 13.868 1.000 26.11 ATOM 1926 CA ILE B 15 104.313 20.975 13.264 1.000 24.37 ATOM 1927 CB ILE B 15 104.478 22.167 12.296 1.000 26.30 ATOM 1928 CG2 ILE B 15 103.173 22.574 11.630 1.000 22.89 ATOM 1929 CG1 ILE B 15 105.139 23.381 12.966 1.000 25.67 ATOM 1930 CD1 ILE B 15 105.607 24.422 11.979 1.000 30.46 ATOM 1931 C ILE B 15 103.704 19.784 12.549 1.000 23.69 ATOM 1932 O ILE B 15 104.196 19.329 11.517 1.000 22.43 ATOM 1933 N THR B 16 102.611 19.249 13.089 1.000 22.07 ATOM 1934 CA THR B 16 101.905 18.147 12.451 1.000 22.03 ATOM 1935 CB THR B 16 101.071 17.349 13.471 1.000 21.22 ATOM 1936 OG1 THR B 16 99.840 18.027 13.733 1.000 23.42 ATOM 1937 CG2 THR B 16 101.799 17.252 14.806 1.000 16.43 ATOM 1938 C THR B 16 101.012 18.664 11.324 1.000 17.32 ATOM 1939 O THR B 16 100.520 19.792 11.351 1.000 22.26 ATOM 1940 N GLY B 17 100.795 17.843 10.306 1.000 20.98 ATOM 1941 CA GLY B 17 100.165 18.276 9.067 1.000 21.27 ATOM 1942 C GLY B 17 101.035 19.294 8.350 1.000 25.39 ATOM 1943 O GLY B 17 100.598 20.121 7.545 1.000 22.63 ATOM 1944 N GLY B 18 102.337 19.254 8.646 1.000 23.37 ATOM 1945 CA GLY B 18 103.254 20.254 8.127 1.000 20.34 ATOM 1946 C GLY B 18 103.480 20.154 6.629 1.000 21.06 ATOM 1947 O GLY B 18 104.077 21.066 6.057 1.000 22.45 ATOM 1948 N ALA B 19 103.026 19.092 5.966 1.000 21.71 ATOM 1949 CA ALA B 19 103.241 18.974 4.525 1.000 23.71 ATOM 1950 CB ALA B 19 103.100 17.520 4.099 1.000 21.03 ATOM 1951 C ALA B 19 102.286 19.849 3.726 1.000 29.96 ATOM 1952 O ALA B 19 102.472 20.117 2.538 1.000 27.73 ATOM 1953 N SER B 20 101.225 20.333 4.367 1.000 23.76 ATOM 1954 CA SER B 20 100.184 21.004 3.590 1.000 22.85 ATOM 1955 CB SER B 20 99.207 19.923 3.103 1.000 26.71 ATOM 1956 OG SER B 20 98.093 20.470 2.425 1.000 31.44 ATOM 1957 C SER B 20 99.454 22.065 4.395 1.000 29.26 ATOM 1958 O SER B 20 99.625 22.195 5.609 1.000 27.20 ATOM 1959 N GLY B 21 98.634 22.827 3.687 1.000 26.85 ATOM 1960 CA GLY B 21 97.667 23.751 4.207 1.000 22.83 ATOM 1961 C GLY B 21 98.094 24.570 5.391 1.000 26.72 ATOM 1962 O GLY B 21 99.054 25.337 5.312 1.000 19.24 ATOM 1963 N LEU B 22 97.365 24.441 6.509 1.000 22.57 ATOM 1964 CA LEU B 22 97.659 25.336 7.627 1.000 22.91 ATOM 1965 CB LEU B 22 96.548 25.233 8.679 1.000 24.42 ATOM 1966 CG LEU B 22 95.151 25.647 8.208 1.000 20.85 ATOM 1967 CD1 LEU B 22 94.133 25.482 9.327 1.000 15.35 ATOM 1968 CD2 LEU B 22 95.161 27.077 7.699 1.000 20.68 ATOM 1969 C LEU B 22 99.028 25.041 8.237 1.000 19.89 ATOM 1970 O LEU B 22 99.782 25.970 8.539 1.000 25.67 ATOM 1971 N GLY B 23 99.359 23.766 8.424 1.000 22.60 ATOM 1972 CA GLY B 23 100.651 23.436 9.030 1.000 27.37 ATOM 1973 C GLY B 23 101.807 23.934 8.185 1.000 25.30 ATOM 1974 O GLY B 23 102.762 24.548 8.660 1.000 21.48 ATOM 1975 N LEU B 24 101.703 23.677 6.878 1.000 23.68 ATOM 1976 CA LEU B 24 102.735 24.155 5.959 1.000 20.25 ATOM 1977 CB LEU B 24 102.420 23.731 4.528 1.000 21.69 ATOM 1978 CG LEU B 24 103.390 24.209 3.444 1.000 23.32 ATOM 1979 CD1 LEU B 24 104.833 23.871 3.784 1.000 23.41 ATOM 1980 CD2 LEU B 24 103.000 23.591 2.103 1.000 25.33 ATOM 1981 C LEU B 24 102.892 25.663 6.030 1.000 20.67 ATOM 1982 O LEU B 24 104.013 26.176 6.115 1.000 24.35 ATOM 1983 N ALA B 25 101.772 26.390 6.006 1.000 24.78 ATOM 1984 CA ALA B 25 101.832 27.851 6.098 1.000 20.17 ATOM 1985 CB ALA B 25 100.444 28.459 6.025 1.000 18.79 ATOM 1986 C ALA B 25 102.528 28.289 7.381 1.000 24.83 ATOM 1987 O ALA B 25 103.263 29.274 7.409 1.000 27.08 ATOM 1988 N THR B 26 102.283 27.539 8.455 1.000 23.74 ATOM 1989 CA THR B 26 102.908 27.892 9.733 1.000 23.95 ATOM 1990 CB THR B 26 102.271 27.065 10.862 1.000 27.15 ATOM 1991 OG1 THR B 26 100.870 27.390 10.918 1.000 20.96 ATOM 1992 CG2 THR B 26 102.862 27.405 12.213 1.000 14.50 ATOM 1993 C THR B 26 104.415 27.688 9.653 1.000 21.31 ATOM 1994 O THR B 26 105.202 28.552 10.040 1.000 23.66 ATOM 1995 N ALA B 27 104.825 26.540 9.126 1.000 19.96 ATOM 1996 CA ALA B 27 106.248 26.260 8.935 1.000 25.17 ATOM 1997 CB ALA B 27 106.418 24.912 8.249 1.000 25.01 ATOM 1998 C ALA B 27 106.931 27.354 8.126 1.000 26.74 ATOM 1999 O ALA B 27 107.949 27.905 8.542 1.000 27.61 ATOM 2000 N GLU B 28 106.372 27.679 6.963 1.000 24.69 ATOM 2001 CA GLU B 28 106.950 28.704 6.105 1.000 25.04 ATOM 2002 CB GLU B 28 106.027 28.975 4.911 1.000 26.62 ATOM 2003 CG GLU B 28 106.168 27.956 3.796 1.000 29.46 ATOM 2004 CD GLU B 28 105.090 28.019 2.739 1.000 34.48 ATOM 2005 OE1 GLU B 28 105.230 27.290 1.733 1.000 37.01 ATOM 2006 OE2 GLU B 28 104.104 28.772 2.894 1.000 38.70 ATOM 2007 C GLU B 28 107.196 29.999 6.861 1.000 28.38 ATOM 2008 O GLU B 28 108.280 30.567 6.830 1.000 22.48 ATOM 2009 N ARG B 29 106.170 30.468 7.572 1.000 26.36 ATOM 2010 CA ARG B 29 106.300 31.722 8.295 1.000 27.51 ATOM 2011 CB ARG B 29 104.930 32.181 8.837 1.000 22.39 ATOM 2012 CG ARG B 29 105.045 33.565 9.447 1.000 23.62 ATOM 2013 CD ARG B 29 103.721 34.034 10.040 1.000 26.86 ATOM 2014 NE ARG B 29 103.902 35.402 10.544 1.000 28.00 ATOM 2015 CZ ARG B 29 103.723 36.469 9.770 1.000 30.37 ATOM 2016 NE1 ARG B 29 103.907 37.674 10.276 1.000 29.53 ATOM 2017 NH2 ARG B 29 103.359 36.297 8.506 1.000 28.65 ATOM 2018 C ARG B 29 107.291 31.618 9.444 1.000 28.71 ATOM 2019 Oo ARG B 29 108.116 32.510 9.652 1.000 29.86 ATOM 2020 N LEU B 30 107.236 30.533 10.224 1.000 24.31 ATOM 2021 CA LEU B 30 108.179 30.478 11.349 1.000 26.41 ATOM 2022 CB LEU B 30 107.813 29.347 12.302 1.000 23.96 ATOM 2023 CG LEU B 30 106.436 29.430 12.973 1.000 23.79 ATOM 2024 CD1 LEU B 30 106.267 28.268 13.944 1.000 17.95 ATOM 2025 CD2 LEU B 30 106.228 30.765 13.668 1.000 24.22 ATOM 2026 C LEU B 30 109.616 30.343 10.853 1.000 31.93 ATOM 2027 O LEU B 30 110.527 31.003 11.357 1.000 30.60 ATOM 2028 N VAL B 31 109.840 29.485 9.858 1.000 26.74 ATOM 2029 CA VAL B 31 111.190 29.383 9.287 1.000 31.33 ATOM 2030 CB VAL B 31 111.255 28.275 8.221 1.000 34.12 ATOM 2031 CG1 VAL B 31 112.445 28.443 7.291 1.000 40.80 ATOM 2032 CG2 VAL B 31 111.305 26.915 8.908 1.000 27.68 ATOM 2033 C VAL B 31 111.609 30.722 8.705 1.000 32.48 ATOM 2034 O VAL B 31 112.725 31.203 8.897 1.000 33.88 ATOM 2035 N GLY B 32 110.692 31.370 7.982 1.000 24.58 ATOM 2036 CA GLY B 32 110.995 32.685 7.451 1.000 26.48 ATOM 2037 C GLY B 32 111.368 33.677 8.531 1.000 33.49 ATOM 2038 O GLY B 32 112.062 34.657 8.266 1.000 31.55 ATOM 2039 N GLN B 33 110.918 33.443 9.760 1.000 37.11 ATOM 2040 CA GLN B 33 111.183 34.351 10.868 1.000 35.69 ATOM 2041 CB GLN B 33 109.978 34.440 11.811 1.000 41.00 ATOM 2042 CG GLN B 33 108.656 34.800 11.155 1.000 43.78 ATOM 2043 CD GLN B 33 108.409 36.287 11.106 1.000 45.96 ATOM 2044 OE1 GLN B 33 108.660 36.975 12.095 1.000 56.75 ATOM 2045 NE2 GLN B 33 107.927 36.777 9.972 1.000 58.65 ATOM 2046 C GLN B 33 112.390 33.917 11.688 1.000 33.13 ATOM 2047 O GLN B 33 112.636 34.505 12.745 1.000 32.32 ATOM 2048 N GLY B 34 113.148 32.913 11.256 1.000 30.65 ATOM 2049 CA GLY B 34 114.338 32.544 12.011 1.000 30.69 ATOM 2050 C GLY B 34 114.173 31.350 12.916 1.000 33.53 ATOM 2051 O GLY B 34 115.124 30.941 13.593 1.000 34.90 ATOM 2052 N ALA B 35 112.994 30.732 12.972 1.000 28.17 ATOM 2053 CA ALA B 35 112.817 29.534 13.781 1.000 24.02 ATOM 2054 CB ALA B 35 111.343 29.442 14.168 1.000 27.36 ATOM 2055 C ALA B 35 113.262 28.268 13.064 1.000 24.80 ATOM 2056 O ALA B 35 113.543 28.284 11.863 1.000 29.10 ATOM 2057 N SER B 36 113.339 27.139 13.766 1.000 21.95 ATOM 2058 CA SER B 36 113.601 25.861 13.109 1.000 31.07 ATOM 2059 CB SER B 36 114.705 25.069 13.814 1.000 28.05 ATOM 2060 OG SER B 36 115.900 25.829 13.875 1.000 35.09 ATOM 2061 C SER B 36 112.323 25.037 13.067 1.000 33.10 ATOM 2062 O SER B 36 111.495 25.123 13.982 1.000 29.14 ATOM 2063 N ALA B 37 112.102 24.227 12.030 1.000 28.97 ATOM 2064 CA ALA B 37 110.812 23.522 12.032 1.000 28.78 ATOM 2065 CB ALA B 37 109.801 24.213 11.123 1.000 28.35 ATOM 2066 C ALA B 37 110.956 22.066 11.632 1.000 28.14 ATOM 2067 O ALA B 37 111.725 21.696 10.746 1.000 31.18 ATOM 2068 N VAL B 38 110.170 21.241 12.323 1.000 2S.45 ATOM 2069 CA VAL B 38 110.026 19.846 11.961 1.000 22.16 ATOM 2070 CB VAL B 38 110.207 18.872 13.132 1.000 25.04 ATOM 2071 CD1 VAL B 38 110.049 17.452 12.602 1.000 24.40 ATOM 2072 CG2 VAL B 38 111.554 19.045 13.807 1.000 33.39 ATOM 2073 C VAL B 38 108.629 19.628 11.377 1.000 27.42 ATOM 2074 O VAL B 38 107.645 19.860 12.081 1.000 28.93 ATOM 2075 N LEU B 39 108.584 19.205 10.125 1.000 26.52 ATOM 2076 CA LEU B 39 107.331 18.890 9.462 1.000 25.31 ATOM 2077 CB LEU B 39 107.440 19.084 7.947 1.000 22.95 ATOM 2078 CG LEU B 39 108.057 20.391 7.464 1.000 21.80 ATOM 2079 CD1 LEU B 39 107.904 20.508 5.951 1.000 22.36 ATOM 2080 CD2 LEU B 39 107.425 21.579 8.178 1.000 22.97 ATOM 2081 C LEU B 39 106.914 17.455 9.749 1.000 25.46 ATOM 2082 O LEU B 39 107.489 16.500 9.232 1.000 26.63 ATOM 2083 N LEU B 40 105.897 17.315 10.591 1.000 23.83 ATOM 2084 CA LEU B 40 105.426 15.985 10.972 1.000 21.42 ATOM 2085 CB LEU B 40 105.097 15.966 12.470 1.000 18.48 ATOM 2086 CG LEU B 40 105.036 14.599 13.150 1.000 25.45 ATOM 2087 CD1 LEU B 40 105.258 14.749 14.649 1.000 26.21 ATOM 2088 CD2 LEU B 40 103.719 13.884 12.872 1.000 26.04 ATOM 2089 C LEU B 40 104.218 15.623 10.120 1.000 28.34 ATOM 2090 O LEU B 40 103.156 16.248 10.223 1.000 25.37 ATOM 2091 N ASP B 41 104.353 14.609 9.267 1.000 28.65 ATOM 2092 CA ASP B 41 103.254 14.287 8.354 1.000 26.00 ATOM 2093 CB ASP B 41 103.214 15.303 7.213 1.000 20.92 ATOM 2094 CG ASP B 41 101.812 15.531 6.671 1.000 29.64 ATOM 2095 OD1 ASP B 41 101.105 14.524 6.429 1.000 27.42 ATOM 2096 OD2 ASP B 41 101.405 16.703 6.478 1.000 26.42 ATOM 2097 C ASP B 41 103.396 12.858 7.850 1.000 29.93 ATOM 2098 O ASP B 41 104.359 12.163 8.188 1.000 26.42 ATOM 2099 N LEU B 42 102.437 12.392 7.051 1.000 28.41 ATOM 2100 CA LEU B 42 102.481 11.005 6.581 1.000 27.15 ATOM 2101 CB LEU B 42 101.108 10.576 6.063 1.000 27.77 ATOM 2102 CG LEU B 42 99.985 10.577 7.115 1.000 29.61 ATOM 2103 CD1 LEU B 42 98.614 10.414 6.481 1.000 27.21 ATOM 2104 CD2 LEU B 42 100.221 9.488 8.154 1.000 19.92 ATOM 2105 C LEU B 42 103.574 10.841 5.531 1.000 25.47 ATOM 2106 O LEU B 42 103.937 11.779 4.822 1.000 22.04 ATOM 2107 N PRO B 43 104.122 9.639 5.436 1.000 29.99 ATOM 2108 CD PRO B 43 103.694 8.435 6.176 1.000 32.56 ATOM 2109 CA PRO B 43 105.242 9.382 4.537 1.000 31.41 ATOM 2110 CB PRO B 43 105.524 7.885 4.706 1.000 29.49 ATOM 2111 CG PRO B 43 104.804 7.459 5.934 1.000 32.19 ATOM 2112 C PRO B 43 104.892 9.640 3.079 1.000 32.37 ATOM 2113 O PRO B 43 105.741 10.056 2.290 1.000 40.08 ATOM 2114 N ASN B 44 103.649 9.379 2.688 1.000 32.25 ATOM 2115 CA ASN B 44 103.351 9.437 1.251 1.000 42.24 ATOM 2116 CB ASN B 44 102.182 8.494 0.942 1.000 51.15 ATOM 2117 CG ASN B 44 101.098 8.594 2.004 1.000 57.16 ATOM 2118 OD1 ASN B 44 101.059 7.778 2.927 1.000 69.55 ATOM 2119 ND2 ASN B 44 100.233 9.594 1.871 1.000 64.33 ATOM 2120 C ASN B 44 103.050 10.848 0.782 1.000 38.90 ATOM 2121 O ASN B 44 102.817 11.126 −0.391 1.000 43.08 ATOM 2122 N SER B 45 103.044 11.795 1.706 1.000 38.17 ATOM 2123 CA SER B 45 102.784 13.191 1.397 1.000 32.01 ATOM 2124 CB SER B 45 102.407 13.904 2.699 1.000 32.03 ATOM 2125 OG SER B 45 103.500 13.896 3.615 1.000 31.99 ATOM 2126 C SER B 45 104.006 13.834 0.765 1.000 37.39 ATOM 2127 O SER B 45 105.029 13.173 0.571 1.000 64.10 ATOM 2128 N GLY B 46 103.940 15.127 0.453 1.000 31.91 ATOM 2129 CA GLY B 46 105.100 15.848 −0.037 1.000 32.05 ATOM 2130 C GLY B 46 105.862 16.554 1.068 1.000 29.66 ATOM 2131 O GLY B 46 106.422 17.629 0.865 1.000 28.80 ATOM 2132 N GLY B 47 105.917 15.984 2.274 1.000 27.32 ATOM 2133 CA GLY B 47 106.644 16.681 3.330 1.000 30.59 ATOM 2134 C GLY B 47 108.119 16.856 3.032 1.000 33.46 ATOM 2135 O GLY B 47 108.684 17.915 3.326 1.000 29.47 ATOM 2136 N GLD B 48 108.764 15.832 2.466 1.000 29.78 ATOM 2137 CA GLU B 48 110.212 15.914 2.232 1.000 32.49 ATOM 2138 CB GLU B 48 110.744 14.610 1.647 1.000 36.34 ATOM 2139 CG GLU B 48 112.256 14.551 1.507 1.000 46.76 ATOM 2140 CD GLU B 48 112.991 14.939 2.774 1.000 58.39 ATOM 2141 OE1 GLU B 48 113.372 16.117 2.956 1.000 65.04 ATOM 2142 OE2 GLU B 48 113.207 14.028 3.606 1.000 69.75 ATOM 2143 C GLU B 48 110.524 17.101 1.331 1.000 29.02 ATOM 2144 0 GLU B 48 111.404 17.915 1.607 1.000 34.13 ATOM 2145 N ALA B 49 109.785 17.216 0.234 1.000 26.82 ATOM 2146 CA ALA B 49 110.004 18.341 −0.673 1.000 30.63 ATOM 2147 CB ALA B 49 109.092 18.199 −1.886 1.000 29.53 ATOM 2148 C ALA B 49 109.794 19.675 0.022 1.000 29.76 ATOM 2149 O ALA B 49 110.547 20.635 −0.182 1.000 23.29 ATOM 2150 N GLN B 50 108.761 19.788 0.867 1.000 27.24 ATOM 2151 CA GLN B 50 108.548 21.102 1.495 1.000 25.56 ATOM 2152 CB GLN B 50 107.198 21.202 2.190 1.000 23.47 ATOM 2153 CG GLN B 50 105.977 20.906 1.343 1.000 24.08 ATOM 2154 CD GLN B 50 105.804 21.782 0.126 1.000 29.27 ATOM 2155 OE1 GLN B 50 105.277 21.374 −0.913 1.000 47.91 ATOM 2156 NE2 GLN B 50 106.246 23.030 0.225 1.000 26.60 ATOM 2157 C GLN B 50 109.685 21.407 2.470 1.000 24.41 ATOM 2158 O GLN B 50 110.136 22.545 2.584 1.000 24.06 ATOM 2159 N ALA B 51 110.164 20.382 3.167 1.000 26.27 ATOM 2160 CA ALA B 51 111.284 20.572 4.092 1.000 28.44 ATOM 2161 CB ALA B 51 111.492 19.317 4.921 1.000 27.41 ATOM 2162 C ALA B 51 112.549 20.947 3.328 1.000 31.71 ATOM 2163 O ALA B 51 113.313 21.838 3.699 1.000 26.46 ATOM 2164 N LYS B 52 112.792 20.260 2.206 1.000 31.97 ATOM 2165 CA LYS B 52 113.941 20.629 1.370 1.000 32.72 ATOM 2166 CB LYS B 52 114.046 19.675 0.190 1.000 37.57 ATOM 2167 CG LYS B 52 114.741 20.219 −1.041 1.000 48.41 ATOM 2168 CD LY5 B 52 113.843 20.066 −2.266 1.000 61.11 ATOM 2169 CE LY5 B 52 112.614 20.953 −2.133 1.000 65.36 ATOM 2170 NZ LY5 B 52 111.536 20.598 −3.095 1.000 32.81 ATOM 2171 C LY5 B 52 113.812 22.074 0.919 1.000 31.76 ATOM 2172 O LY5 B 52 114.749 22.872 1.011 1.000 30.51 ATOM 2173 N LY5 B 53 112.625 22.447 0.436 1.000 30.99 ATOM 2174 CA LY5 B 53 112.430 23.823 −0.007 1.000 34.36 ATOM 2175 CB LY5 B 53 111.017 24.015 −0.558 1.000 35.38 ATOM 2176 C LY5 B 53 112.670 24.835 1.104 1.000 35.83 ATOM 2177 O LY5 B 53 113.099 25.966 0.863 1.000 37.38 ATOM 2178 N LEU B 54 112.376 24.467 2.355 1.000 34.60 ATOM 2179 CA LEU B 54 112.414 25.524 3.378 1.000 32.04 ATOM 2180 CB LEU B 54 111.386 25.206 4.469 1.000 27.56 ATOM 2181 CG LEU B 54 109.951 25.622 4.092 1.000 29.64 ATOM 2182 CD1 LEU B 54 108.940 25.049 5.072 1.000 26.83 ATOM 2183 CD2 LEU B 54 109.854 27.139 4.005 1.000 28.08 ATOM 2184 C LEU B 54 113.803 25.751 3.946 1.000 30.99 ATOM 2185 O LEU B 54 114.035 26.722 4.670 1.000 36.53 ATOM 2186 N GLY B 55 114.760 24.889 3.613 1.000 35.24 ATOM 2187 CA GLY B 55 116.145 25.129 3.970 1.000 28.30 ATOM 2188 C GLY B 55 116.658 24.251 5.088 1.000 28.98 ATOM 2189 O GLY B 55 115.983 23.344 5.577 1.000 26.51 ATOM 2190 N A5N B 56 117.886 24.525 5.500 1.000 31.16 ATOM 2191 CA A5N B 56 118.579 23.765 6.527 1.000 37.68 ATOM 2192 CB A5N B 56 120.017 24.285 6.673 1.000 45.44 ATOM 2193 CG A5N B 56 120.802 24.041 5.394 1.000 53.62 ATOM 2194 OD1 A5N B 56 121.666 24.836 5.028 1.000 63.23 ATOM 2195 ND2 A5N B 56 120.488 22.943 4.713 1.000 51.47 ATOM 2196 C A5N B 56 117.884 23.822 7.876 1.000 35.34 ATOM 2197 O A5N B 56 118.077 22.918 8.695 1.000 36.61 ATOM 2198 N A5N B 57 117.080 24.852 8.124 1.000 35.84 ATOM 2199 CA A5N B 57 116.390 24.941 9.415 1.000 33.51 ATOM 2200 CB A5N B 57 116.150 26.402 9.776 1.000 34.67 ATOM 2201 CG A5N B 57 117.396 27.188 10.107 1.000 37.48 ATOM 2202 OD1 A5N B 57 117.464 28.386 9.831 1.000 44.60 ATOM 2203 ND2 A5N B 57 118.378 26.525 10.702 1.000 40.04 ATOM 2204 C A5N B 57 115.062 24.188 9.411 1.000 34.71 ATOM 2205 O A5N B 57 114.259 24.325 10.339 1.000 30.75 ATOM 2206 N CY5 B 58 114.815 23.385 8.381 1.000 29.69 ATOM 2207 CA CY5 B 58 113.570 22.626 8.314 1.000 31.12 ATOM 2208 CB CY5 B 58 112.554 23.328 7.403 1.000 28.69 ATOM 2209 5G CY5 B 58 110.969 22.451 7.263 1.000 28.53 ATOM 2210 C CYS B 58 113.803 21.196 7.842 1.000 29.28 ATOM 2211 O CYS B 58 114.439 20.961 6.813 1.000 32.21 ATOM 2212 N VAL B 59 113.295 20.221 8.587 1.000 26.05 ATOM 2213 CA VAL B 59 113.388 18.827 8.185 1.000 27.33 ATOM 2214 CB VAL B 59 114.370 18.032 9.068 1.000 35.06 ATOM 2215 CG1 VAL B 59 115.723 18.727 9.136 1.000 33.58 ATOM 2216 CG2 VAL B 59 113.819 17.829 10.473 1.000 34.14 ATOM 2217 C VAL B 59 112.021 18.148 8.226 1.000 27.96 ATOM 2218 O VAL B 59 111.077 18.615 8.868 1.000 29.69 ATOM 2219 N PHE B 60 111.910 17.034 7.523 1.000 26.97 ATOM 2220 CA PHE B 60 110.708 16.227 7.457 1.000 26.91 ATOM 2221 CB PEE B 60 110.427 15.790 6.020 1.000 25.25 ATOM 2222 CG PHE B 60 109.323 14.749 5.896 1.000 29.29 ATOM 2223 CD1 PHE B 60 108.032 15.040 6.313 1.000 29.86 ATOM 2224 CD2 PHE B 60 109.578 13.496 5.370 1.000 28.92 ATOM 2225 CE1 PHE B 60 107.038 14.090 6.198 1.000 27.49 ATOM 2226 CE2 PHE B 60 108.586 12.541 5.248 1.000 26.44 ATOM 2227 CZ PHE B 60 107.300 12.839 5.667 1.000 25.34 ATOM 2228 C PHE B 60 110.830 14.998 8.353 1.000 30.94 ATOM 2229 O PHE B 60 111.820 14.270 8.314 1.000 25.53 ATOM 2230 N ALA B 61 109.800 14.783 9.167 1.000 28.55 ATOM 2231 CA ALA B 61 109.720 13.601 10.013 1.000 25.87 ATOM 2232 CB ALA B 61 109.776 13.997 11.480 1.000 26.71 ATOM 2233 C ALA B 61 108.444 12.838 9.687 1.000 27.90 ATOM 2234 O ALA B 61 107.358 13.292 10.060 1.000 32.37 ATOM 2235 N PRO B 62 108.554 11.718 8.984 1.000 30.44 ATOM 2236 CD PRO B 62 109.781 11.150 8.400 1.000 27.89 ATOM 2237 CA PRO B 62 107.376 10.900 8.679 1.000 29.03 ATOM 2238 CB PRO B 62 107.922 9.757 7.816 1.000 28.20 ATOM 2239 CG PRO B 62 109.385 9.732 8.097 1.000 28.71 ATOM 2240 C PRO B 62 106.750 10.325 9.944 1.000 29.30 ATOM 2241 O PRO B 62 107.417 9.731 10.789 1.000 30.53 ATOM 2242 N ALA B 63 105.439 10.485 10.095 1.000 27.18 ATOM 2243 CA ALA B 63 104.766 9.913 11.259 1.000 27.63 ATOM 2244 CB ALA B 63 105.180 10.646 12.524 1.000 23.24 ATOM 2245 C ALA B 63 103.249 9.974 11.099 1.000 23.37 ATOM 2246 O ALA B 63 102.722 10.929 10.526 1.000 27.56 ATOM 2247 N ASP B 64 102.583 8.953 11.609 1.000 24.35 ATOM 2248 CA ASP B 64 101.133 8.963 11.799 1.000 26.55 ATOM 2249 CB ASP B 64 100.551 7.597 11.478 1.000 24.92 ATOM 2250 CG ASP B 64 99.045 7.527 11.597 1.000 25.45 ATOM 2251 OD1 ASP B 64 98.476 6.566 11.044 1.000 32.77 ATOM 2252 OD2 ASP B 64 98.418 8.396 12.227 1.000 28.70 ATOM 2253 C ASP B 64 100.836 9.364 13.243 1.000 26.22 ATOM 2254 O ASP B 64 101.328 8.686 14.153 1.000 22.25 ATOM 2255 N VAL B 65 100.072 10.435 13.456 1.000 29.99 ATOM 2256 CA VAL B 65 99.881 10.939 14.821 1.000 24.56 ATOM 2257 CB VAL B 65 99.246 12.340 14.882 1.000 24.64 ATOM 2258 CG1 VAL B 65 100.144 13.380 14.212 1.000 20.71 ATOM 2259 CG2 VAL B 65 97.855 12.336 14.260 1.000 19.79 ATOM 2260 C VAL B 65 99.029 9.988 15.655 1.000 21.85 ATOM 2261 O VAL B 65 98.984 10.127 16.883 1.000 27.56 ATOM 2262 N TSR B 66 98.358 9.029 15.024 1.000 18.06 ATOM 2263 CA TSR B 66 97.587 8.071 15.806 1.000 23.90 ATOM 2264 CB TSR B 66 96.458 7.415 14.988 1.000 27.89 ATOM 2265 OD1 TSR B 66 97.053 6.676 13.911 1.000 30.40 ATOM 2266 CG2 TSR B 66 95.531 8.457 14.387 1.000 26.02 ATOM 2267 C TSR B 66 98.477 6.956 16.354 1.000 25.80 ATOM 2268 O TSR B 66 97.994 6.069 17.052 1.000 28.04 ATOM 2269 N SER B 67 99.765 6.987 16.043 1.000 26.27 ATOM 2270 CA SER B 67 100.658 5.901 16.457 1.000 28.10 ATOM 2271 CB SER B 67 101.309 5.256 15.229 1.000 22.33 ATOM 2272 OG SER B 67 102.655 4.885 15.432 1.000 26.97 ATOM 2273 CB SER B 67 101.718 6.397 17.438 1.000 25.97 ATOM 2274 O SER B 67 102.509 7.2881 7.137 1.000 28.64 ATOM 2275 N GLU B 68 101.742 5.8121 8.628 1.000 25.20 ATOM 2276 CA GLU B 68 102.668 6.2401 9.678 1.000 28.93 ATOM 2277 CB GLU B 68 102.418 5.401 20.920 1.000 29.49 ATOM 2278 CG GLU B 68 103.467 5.385 22.009 1.000 32.30 ATOM 2279 CD GLU B 68 102.977 4.561 23.196 1.000 38.17 ATOM 2280 OE1 GLU B 68 102.637 5.171 24.237 1.000 35.47 ATOM 2281 OE2 GLU B 68 102.917 3.315 23.091 1.000 44.60 ATOM 2282 C GLU B 68 104.110 6.125 19.201 1.000 26.61 ATOM 2283 O GLU B 68 104.899 7.061 19.313 1.000 23.88 ATOM 2284 N LYS B 69 104.437 4.958 18.662 1.000 24.43 ATOM 2285 CA LYS B 69 105.780 4.698 18.156 1.000 27.96 ATOM 2286 CB LYS B 69 105.851 3.281 17.595 1.000 34.89 ATOM 2287 C LYS B 69 106.202 5.708 17.100 1.000 27.55 ATOM 2288 O LYS B 69 107.302 6.264 17.148 1.000 26.09 ATOM 2289 N ASP B 70 105.324 5.973 16.128 1.000 26.32 ATOM 2290 CA ASP B 70 105.666 6.951 15.094 1.000 25.61 ATOM 2291 CB ASP B 70 104.521 7.076 14.090 1.000 29.36 ATOM 2292 CG ASP B 70 104.475 5.972 13.052 1.000 32.02 ATOM 2293 OD1 ASP B 70 105.238 4.989 13.156 1.000 28.74 ATOM 2294 OD2 ASP B 70 103.655 6.078 12.105 1.000 31.35 ATOM 2295 C ASP B 70 105.969 8.310 15.703 1.000 25.58 ATOM 2296 O ASP B 70 106.940 8.988 15.360 1.000 25.97 ATOM 2297 N VAL B 71 105.114 8.758 16.635 1.000 27.46 ATOM 2298 CA VAL B 71 105.340 10.110 17.172 1.000 23.79 ATOM 2299 CB VAL B 71 104.121 10.602 17.966 1.000 23.68 ATOM 2300 CD1 VAL B 71 104.423 11.915 18.668 1.000 22.16 ATOM 2301 CG2 VAL B 71 102.929 10.759 17.030 1.000 27.40 ATOM 2302 C VAL B 71 106.598 10.124 18.025 1.000 23.50 ATOM 2303 O VAL B 71 107.373 11.079 18.014 1.000 25.44 ATOM 2304 N GLN B 72 106.808 9.037 18.777 1.000 22.76 ATOM 2305 CA GLN B 72 108.078 8.961 19.507 1.000 28.52 ATOM 2306 CB GLN B 72 108.135 7.661 20.313 1.000 28.51 ATOM 2307 CG GLN B 72 107.370 7.770 21.621 1.000 29.69 ATOM 2308 CD GLN B 72 107.251 6.451 22.355 1.000 35.53 ATOM 2309 OE1 GLN B 72 106.976 5.411 21.762 1.000 42.43 ATOM 2310 NE2 GLN B 72 107.450 6.507 23.669 1.000 42.60 ATOM 2311 C GLN B 72 109.238 9.055 18.532 1.000 27.07 ATOM 2312 O GLN B 72 110.206 9.781 18.738 1.000 30.00 ATOM 2313 N THR B 73 109.126 8.301 17.432 1.000 23.90 ATOM 2314 CA THR B 73 110.180 8.335 16.419 1.000 30.39 ATOM 2315 CB THR B 73 109.809 7.402 15.245 1.000 37.28 ATOM 2316 OG1 THR B 73 109.774 6.051 15.729 1.000 35.29 ATOM 2317 CG2 THR B 73 110.846 7.464 14.138 1.000 35.54 ATOM 2318 C THR B 73 110.426 9.744 15.905 1.000 31.92 ATOM 2319 O THR B 73 111.559 10.226 15.830 1.000 33.51 ATOM 2320 N ALA B 74 109.341 10.436 15.545 1.000 27.80 ATOM 2321 CA ALA B 74 109.484 11.799 15.050 1.000 22.69 ATOM 2322 CB ALA B 74 108.134 12.322 14.574 1.000 23.30 ATOM 2323 C ALA B 74 110.074 12.723 16.102 1.000 26.52 ATOM 2324 O ALA B 74 110.869 13.610 15.783 1.000 29.72 ATOM 2325 N LEU B 75 109.701 12.558 17.374 1.000 25.95 ATOM 2326 CA LEU B 75 110.234 13.504 18.364 1.000 25.51 ATOM 2327 CB LEU B 75 109.399 13.416 19.648 1.000 26.48 ATOM 2328 CG LEU B 75 107.994 14.018 19.562 1.000 24.78 ATOM 2329 CD1 LEU B 75 107.305 13.969 20.919 1.000 28.37 ATOM 2330 CD2 LEU B 75 108.043 15.449 19.050 1.000 24.31 ATOM 2331 C LEU B 75 111.705 13.245 18.648 1.000 22.87 ATOM 2332 O LEU B 75 112.509 14.147 18.887 1.000 22.28 ATOM 2333 N ALA B 76 112.089 11.972 18.627 1.000 27.27 ATOM 2334 CA ALA B 76 113.506 11.626 18.780 1.000 33.68 ATOM 2335 CB ALA B 76 113.673 10.117 18.844 1.000 30.02 ATOM 2336 C ALA B 76 114.318 12.238 17.643 1.000 34.38 ATOM 2337 O ALA B 76 115.423 12.735 17.830 1.000 32.44 ATOM 2338 N LEU B 77 113.746 12.211 16.439 1.000 35.72 ATOM 2339 CA LEU B 77 114.406 12.813 15.279 1.000 29.98 ATOM 2340 CB LEU B 77 113.597 12.512 14.022 1.000 32.18 ATOM 2341 CG LEU B 77 114.232 12.800 12.666 1.000 35.08 ATOM 2342 CD1 LEU B 77 113.659 11.860 11.611 1.000 41.62 ATOM 2343 CD2 LEU B 77 114.033 14.245 12.241 1.000 32.26 ATOM 2344 C LEU B 77 114.574 14.310 15.481 1.000 31.25 ATOM 2345 O LEU B 77 115.606 14.894 15.149 1.000 31.59 ATOM 2346 N ALA B 78 113.541 14.968 16.013 1.000 29.31 ATOM 2347 CA ALA B 78 113.645 16.414 16.212 1.000 29.75 ATOM 2348 CB ALA B 78 112.313 17.019 16.619 1.000 30.45 ATOM 2349 C ALA B 78 114.710 16.745 17.249 1.000 28.71 ATOM 2350 O ALA B 78 115.502 17.670 17.063 1.000 27.61 ATOM 2351 N LYS B 79 114.745 16.003 18.357 1.000 33.16 ATOM 2352 CA LYS B 79 115.778 16.335 19.354 1.000 38.43 ATOM 2353 CB LYS B 79 115.625 15.513 20.619 1.000 31.00 ATOM 2354 C LYS B 79 117.164 16.157 18.731 1.000 38.50 ATOM 2355 O LYS B 79 118.019 17.042 18.730 1.000 37.36 ATOM 2356 N GLY B 80 117.376 14.975 18.163 1.000 38.28 ATOM 2357 CA GLY B 80 118.617 14.652 17.482 1.000 40.37 ATOM 2358 C GLY B 80 118.986 15.682 16.440 1.000 41.82 ATOM 2359 O GLY B 80 120.160 15.985 16.233 1.000 43.44 ATOM 2360 N LYS B 81 117.993 16.265 15.757 1.000 38.61 ATOM 2361 CA LYS B 81 118.386 17.243 14.741 1.000 34.19 ATOM 2362 CB LYS B 81 117.372 17.249 13.592 1.000 39.19 ATOM 2363 CG LYS B 81 117.538 18.427 12.637 1.000 47.35 ATOM 2364 CD LYS B 81 118.642 18.163 11.626 1.000 53.28 ATOM 2365 CE LYS B 81 119.342 19.448 11.209 1.000 57.14 ATOM 2366 NZ LYS B 81 120.217 19.236 10.022 1.000 61.45 ATOM 2367 C LYS B 81 118.543 18.637 15.322 1.000 35.44 ATOM 2368 O LYS B 81 119.491 19.336 14.958 1.000 32.57 ATOM 2369 N PHE B 82 117.643 19.075 16.201 1.000 33.67 ATOM 2370 CA PHE B 82 117.687 20.471 16.628 1.000 30.79 ATOM 2371 CB PHE B 82 116.404 21.198 16.219 1.000 33.81 ATOM 2372 CG PHE B 82 116.254 21.364 14.714 1.000 34.04 ATOM 2373 CD1 PHE B 82 117.213 22.049 13.985 1.000 32.49 ATOM 2374 CD2 PHE B 82 115.157 20.833 14.049 1.000 31.02 ATOM 2375 CE1 PHE B 82 117.09 322.203 12.616 1.000 33.17 ATOM 2376 CE2 PHE B 82 115.030 20.985 12.682 1.000 29.68 ATOM 2377 CZ PHE B 82 115.996 21.669 11.963 1.000 33.22 ATOM 2378 C PHE B 82 117.902 20.639 18.128 1.000 34.16 ATOM 2379 O PHE B 82 117.977 21.775 18.604 1.000 34.38 ATOM 2380 N GLY B 83 118.015 19.535 18.859 1.000 36.21 ATOM 2381 CA GLY B 83 118.420 19.550 20.240 1.000 37.95 ATOM 2382 C GLY B 83 117.354 19.747 21.287 1.000 40.28 ATOM 2383 O GLY B 83 117.569 19.334 22.435 1.000 38.88 ATOM 2384 N ARG B 84 116.230 20.361 20.947 1.000 37.13 ATOM 2385 CA ARG B 84 115.132 20.596 21.879 1.000 33.93 ATOM 2386 CB ARG B 84 115.438 21.715 22.874 1.000 26.55 ATOM 2387 CG ARG B 84 115.871 23.032 22.277 1.000 34.91 ATOM 2388 CD ARG B 84 115.369 24.232 23.062 1.000 45.07 ATOM 2389 NE ARG B 84 115.930 24.340 24.401 1.000 52.33 ATOM 2390 CZ ARG B 84 115.403 24.960 25.444 1.000 56.40 ATOM 2391 NH1 ARG B 84 116.049 24.962 26.607 1.000 64.88 ATOM 2392 NH2 ARG B 84 114.238 25.591 25.372 1.000 32.24 ATOM 2393 C ARG B 84 113.863 20.943 21.102 1.000 35.43 ATOM 2394 O ARG B 84 113.976 21.169 19.893 1.000 38.55 ATOM 2395 N VAL B 85 112.727 20.977 21.792 1.000 25.77 ATOM 2396 CA VAL B 85 111.474 21.435 21.208 1.000 23.25 ATOM 2397 CB VAL B 85 110.453 20.303 21.008 1.000 28.26 ATOM 2398 CG1 VAL B 85 109.205 20.870 20.335 1.000 27.90 ATOM 2399 CG2 VAL B 85 111.018 19.159 20.183 1.000 25.21 ATOM 2400 C VAL B 85 110.836 22.521 22.072 1.000 25.60 ATOM 2401 O VAL B 85 110.606 22.326 23.263 1.000 29.58 ATOM 2402 N ASP B 86 110.541 23.669 21.481 1.000 25.06 ATOM 2403 CA ASP B 86 109.985 24.804 22.195 1.000 24.15 ATOM 2404 CB ASP B 86 110.675 26.098 21.753 1.000 27.61 ATOM 2405 CG ASP B 86 112.183 25.984 21.887 1.000 32.39 ATOM 2406 OD1 ASP B 86 112.882 25.895 20.862 1.000 33.23 ATOM 2407 OD2 ASP B 86 112.610 25.970 23.055 1.000 34.44 ATOM 2408 C ASP B 86 108.490 24.977 21.949 1.000 30.30 ATOM 2409 O ASP B 86 107.788 25.521 22.798 1.000 21.74 ATOM 2410 N VAL B 87 108.059 24.524 20.778 1.000 23.56 ATOM 2411 CA VAL B 87 106.718 24.750 20.265 1.000 19.89 ATOM 2412 CB VAL B 87 106.701 25.920 19.260 1.000 25.46 ATOM 2413 CG1 VAL B 87 105.346 26.049 18.580 1.000 23.92 ATOM 2414 CG2 VAL B 87 107.072 27.232 19.942 1.000 23.79 ATOM 2415 C VAL B 87 106.197 23.506 19.563 1.000 24.56 ATOM 2416 O VAL B 87 106.923 22.816 18.841 1.000 26.61 ATOM 2417 N ALA B 88 104.922 23.211 19.784 1.000 22.40 ATOM 2418 CA ALA B 88 104.242 22.158 19.039 1.000 20.37 ATOM 2419 CB ALA B 88 103.979 20.911 19.848 1.000 19.16 ATOM 2420 C ALA B 88 102.940 22.763 18.508 1.000 25.15 ATOM 2421 O ALA B 88 102.254 23.506 19.204 1.000 23.17 ATOM 2422 N VAL B 89 102.641 22.455 17.254 1.000 23.24 ATOM 2423 CA VAL B 89 101.405 22.908 16.621 1.000 20.62 ATOM 2424 CB VAL B 89 101.617 24.043 15.611 1.000 26.07 ATOM 2425 CG1 VAL B 89 100.278 24.578 15.114 1.000 24.86 ATOM 2426 CG2 VAL B 89 102.426 25.180 16.224 1.000 20.28 ATOM 2427 C VAL B 89 100.760 21.700 15.948 1.000 20.49 ATOM 2428 O VAL B 89 101.390 21.106 15.061 1.000 22.27 ATOM 2429 N ASN B 90 99.564 21.369 16.399 1.000 17.06 ATOM 2430 CA ASN B 90 98.767 20.263 15.895 1.000 21.63 ATOM 2431 CB ASN B 90 97.912 19.676 17.029 1.000 21.17 ATOM 2432 CG ASN B 90 98.770 18.964 18.062 1.000 25.12 ATOM 2433 OD1 ASN B 90 99.010 19.453 19.168 1.000 26.62 ATOM 2434 ND2 ASN B 90 99.248 17.781 17.700 1.000 19.87 ATOM 2435 C ASN B 90 97.873 20.706 14.739 1.000 27.25 ATOM 2436 O ASN B 90 96.831 21.346 14.926 1.000 24.49 ATOM 2437 N CYS B 91 98.272 20.379 13.508 1.000 22.65 ATOM 2438 CA CYS B 91 97.454 20.744 12.352 1.000 22.91 ATOM 2439 CB CYS B 91 98.256 21.622 11.393 1.000 21.50 ATOM 2440 SG CYS B 91 98.481 23.331 11.928 1.000 24.36 ATOM 2441 C CYS B 91 96.938 19.496 11.645 1.000 27.06 ATOM 2442 O CYS B 91 95.978 19.559 10.883 1.000 25.06 ATOM 2443 N ALA B 92 97.568 18.349 11.892 1.000 24.70 ATOM 2444 CA ALA B 92 97.110 17.080 11.342 1.000 26.12 ATOM 2445 CB ALA B 92 97.914 15.933 11.959 1.000 19.70 ATOM 2446 C ALA B 92 95.621 16.872 11.572 1.000 29.63 ATOM 2447 O ALA B 92 95.119 16.947 12.698 1.000 21.23 ATOM 2448 N GLY B 93 94.889 16.609 10.487 1.000 27.75 ATOM 2449 CA GLY B 93 93.457 16.386 10.607 1.000 22.27 ATOM 2450 C GLY B 93 92.818 15.838 9.346 1.000 25.37 ATOM 2451 O GLY B 93 93.385 15.929 8.258 1.000 21.56 ATOM 2452 N ILE B 94 91.632 15.264 9.485 1.000 22.61 ATOM 2453 CA ILE B 94 90.850 14.804 8.346 1.000 24.90 ATOM 2454 CB ILE B 94 90.800 13.273 8.204 1.000 25.11 ATOM 2455 CG2 ILE B 94 92.115 12.706 7.714 1.000 22.97 ATOM 2456 CG1 ILE B 94 90.338 12.560 9.483 1.000 27.64 ATOM 2457 CD1 ILE B 94 89.890 11.131 9.224 1.000 26.94 ATOM 2458 C ILE B 94 89.407 15.295 8.479 1.000 25.32 ATOM 2459 O ILE B 94 88.996 15.736 9.550 1.000 24.04 ATOM 2460 N ALA B 95 88.659 15.202 7.393 1.000 31.39 ATOM 2461 CA ALA B 95 87.265 15.611 7.343 1.000 32.56 ATOM 2462 CB ALA B 95 87.069 16.880 6.525 1.000 25.46 ATOM 2463 C ALA B 95 86.409 14.505 6.746 1.000 32.05 ATOM 2464 O ALA B 95 86.857 13.724 5.912 1.000 26.39 ATOM 2465 N VAL B 96 85.160 14.442 7.191 1.000 27.70 ATOM 2466 CA VAL B 96 84.185 13.607 6.506 1.000 27.20 ATOM 2467 CB VAL B 96 83.957 12.218 7.104 1.000 32.47 ATOM 2468 CG1 VAL B 96 85.263 11.457 7.265 1.000 52.62 ATOM 2469 CG2 VAL B 96 83.244 12.333 8.443 1.000 43.39 ATOM 2470 C VAL B 96 82.857 14.374 6.512 1.000 26.65 ATOM 2471 O VAL B 96 82.617 15.204 7.398 1.000 25.44 ATOM 2472 N ALA B 97 82.047 14.075 5.506 1.000 26.05 ATOM 2473 CA ALA B 97 80.690 14.629 5.475 1.000 22.29 ATOM 2474 CB ALA B 97 80.509 15.590 4.323 1.000 29.01 ATOM 2475 C ALA B 97 79.737 13.442 5.426 1.000 25.57 ATOM 2476 O ALA B 97 79.745 12.662 4.479 1.000 29.16 ATOM 2477 N SER B 98 78.940 13.271 6.469 1.000 21.75 ATOM 2478 CA SER B 98 78.024 12.132 6.535 1.000 25.42 ATOM 2479 CB SER B 98 78.792 10.846 6.799 1.000 26.09 ATOM 2480 OG SER B 98 77.975 9.704 6.960 1.000 23.21 ATOM 2481 CB SER B 98 76.998 12.432 7.626 1.000 28.54 ATOM 2482 O SER B 98 77.383 12.679 8.775 1.000 22.53 ATOM 2483 N LYS B 99 75.731 12.420 7.235 1.000 22.98 ATOM 2484 CA LYS B 99 74.636 12.671 8.162 1.000 26.62 ATOM 2485 CB LYS B 99 73.326 12.836 7.385 1.000 26.24 ATOM 2486 CG LYS B 99 73.276 14.063 6.492 1.000 25.94 ATOM 2487 CD LYS B 99 72.099 13.945 5.534 1.000 32.26 ATOM 2488 CE LYS B 99 71.982 15.187 4.659 1.000 37.24 ATOM 2489 NZ LYS B 99 70.599 15.299 4.106 1.000 50.59 ATOM 2490 C LYS B 99 74.461 11.545 9.181 1.000 27.88 ATOM 2491 O LYS B 99 74.711 10.370 8.884 1.000 21.35 ATOM 2492 N THR B 100 74.007 11.918 10.382 1.000 21.91 ATOM 2493 CA THR B 100 73.801 10.934 11.444 1.000 18.81 ATOM 2494 CB THR B 100 73.223 11.601 12.709 1.000 21.49 ATOM 2495 OG1 THR B 100 74.235 12.450 13.267 1.000 21.98 ATOM 2496 CG2 THR B 100 72.862 10.565 13.755 1.000 18.29 ATOM 2497 C THR B 100 72.873 9.821 10.988 1.000 23.10 ATOM 2498 O THR B 100 73.143 8.635 11.153 1.000 23.86 ATOM 2499 N TYR B 101 71.758 10.242 10.399 1.000 25.05 ATOM 2500 CA TYR B 101 70.827 9.312 9.782 1.000 25.55 ATOM 2501 CB TYR B 101 69.788 8.824 10.801 1.000 24.38 ATOM 2502 CG TYR B 101 68.798 7.861 10.170 1.000 27.81 ATOM 2503 CD1 TYR B 101 67.465 8.207 10.024 1.000 27.63 ATOM 2504 CE1 TYR B 101 66.570 7.330 9.448 1.000 29.00 ATOM 2505 CD2 TYR B 101 69.211 6.614 9.719 1.000 28.85 ATOM 2506 CE2 TYR B 101 68.323 5.730 9.141 1.000 29.92 ATOM 2507 CZ TYR B 101 67.002 6.099 9.010 1.000 32.68 ATOM 2508 OH TYR B 101 66.106 5.224 8.434 1.000 33.84 ATOM 2509 C TYR B 101 70.138 9.977 8.592 1.000 30.29 ATOM 2510 O TYR B 101 69.842 11.171 8.653 1.000 27.66 ATOM 2511 N ASN B 102 69.890 9.219 7.533 1.000 32.30 ATOM 2512 CA ASN B 102 69.095 9.704 6.406 1.000 27.57 ATOM 2513 CB ASN B 102 69.937 9.723 5.130 1.000 33.98 ATOM 2514 CG ASN B 102 69.240 10.469 4.002 1.000 36.11 ATOM 2515 OD1 ASN B 102 68.038 10.287 3.797 1.000 36.21 ATOM 2516 ND2 ASN B 102 69.974 11.311 3.283 1.000 25.79 ATOM 2517 C ASN B 102 67.861 8.827 6.227 1.000 24.40 ATOM 2518 O ASN B 102 67.974 7.665 5.835 1.000 29.49 ATOM 2519 N LEU B 103 66.686 9.356 6.540 1.000 26.99 ATOM 2520 CA LEU B 103 65.448 8.591 6.417 1.000 29.76 ATOM 2521 CB LEU B 103 64.314 9.311 7.147 1.000 29.43 ATOM 2522 CG LEU B 103 62.934 8.653 7.112 1.000 31.78 ATOM 2523 CD1 LEU B 103 62.971 7.289 7.788 1.000 34.16 ATOM 2524 CD2 LEU B B103 61.896 9.556 7.758 1.000 27.01 ATOM 2525 C LEU B 103 65.085 8.367 4.954 1.000 35.54 ATOM 2526 O LEU B 103 64.742 7.255 4.545 1.000 40.20 ATOM 2527 N LYS B 104 65.145 9.416 4.148 1.000 39.57 ATOM 2528 CA LYS B 104 64.863 9.329 2.721 1.000 42.48 ATOM 2529 CB LYS B 104 65.030 10.699 2.075 1.000 51.56 ATOM 2530 C LYS B 104 65.754 8.307 2.024 1.000 39.81 ATOM 2531 O LYS B 104 65.311 7.619 1.101 1.000 43.72 ATOM 2532 N LYS B 105 67.005 8.200 2.467 1.000 35.79 ATOM 2533 CA LYS B 105 67.924 7.211 1.915 1.000 35.08 ATOM 2534 CB LYS B 105 69.362 7.723 1.913 1.000 42.55 ATOM 2535 CG LYS B 105 69.810 8.431 0.648 1.000 52.17 ATOM 2536 CD LYS B 105 71.334 8.483 0.589 1.000 61.85 ATOM 2537 CE LYS B 105 71.944 7.291 1.310 1.000 67.77 ATOM 2538 NZ LYS B 105 73.111 7.657 2.157 1.000 69.80 ATOM 2539 C LYS B 105 67.886 5.909 2.705 1.000 32.76 ATOM 2540 O LYS B 105 68.341 4.878 2.205 1.000 33.06 ATOM 2541 N GLY B 106 67.367 5.936 3.932 1.000 26.52 ATOM 2542 CA GLY B 106 67.455 4.735 4.761 1.000 22.95 ATOM 2543 C GLY B 106 68.881 4.466 5.188 1.000 27.67 ATOM 2544 O GLY B 106 69.268 3.325 5.436 1.000 33.60 ATOM 2545 N GLN B 107 69.706 5.505 5.286 1.000 33.76 ATOM 2546 CA GLN B 107 71.137 5.336 5.486 1.000 30.81 ATOM 2547 CB GLN B 107 71.888 6.022 4.355 1.000 28.84 ATOM 2548 C GLN B 107 71.605 5.873 6.836 1.000 28.73 ATOM 2549 O GLN B 107 71.132 6.916 7.283 1.000 26.22 ATOM 2550 N THR B 108 72.524 5.136 7.439 1.000 28.78 ATOM 2551 CA THR B 108 73.069 5.396 8.764 1.000 30.06 ATOM 2552 CB THR B 108 72.901 4.154 9.665 1.000 27.78 ATOM 2553 OG1 THR B 108 71.501 3.870 9.817 1.000 28.16 ATOM 2554 CG2 THR B 108 73.471 4.405 11.051 1.000 26.31 ATOM 2555 C THR B 108 74.549 5.744 8.708 1.000 27.68 ATOM 2556 O THR B 108 75.304 5.055 8.017 1.000 28.23 ATOM 2557 N HIS B 109 74.971 6.780 9.423 1.000 26.32 ATOM 2558 CA HIS B 109 76.405 7.080 9.530 1.000 24.60 ATOM 2559 CB HIS B 109 76.595 8.232 10.498 1.000 25.11 ATOM 2560 CG HIS B 109 77.918 8.912 10.561 1.000 23.44 ATOM 2561 CD2 HIS B 109 78.226 10.231 10.518 1.000 24.11 ATOM 2562 ND1 HIS B 109 79.116 8.252 10.721 1.000 22.09 ATOM 2563 CE1 HIS B 109 80.103 9.132 10.759 1.000 20.27 ATOM 2564 NE2 HIS B 109 79.593 10.343 10.640 1.000 21.90 ATOM 2565 C HIS B 109 77.151 5.845 9.997 1.000 22.44 ATOM 2566 O HIS B 109 76.727 5.200 10.961 1.000 26.30 ATOM 2567 N THR B 110 78.256 5.471 9.354 1.000 23.04 ATOM 2568 CA THR B 110 78.923 4.256 9.823 1.000 21.12 ATOM 2569 CB THR B 110 79.894 3.654 8.791 1.000 22.73 ATOM 2570 OG1 THR B 110 81.045 4.516 8.728 1.000 25.04 ATOM 2571 CG2 THR B 110 79.256 3.561 7.413 1.000 19.23 ATOM 2572 C THR B 110 79.741 4.515 11.081 1.000 24.40 ATOM 2573 O THR B 110 80.307 5.592 11.265 1.000 31.84 ATOM 2574 N LEU B 111 79.821 3.500 11.937 1.000 27.00 ATOM 2575 CA LEU B 111 80.605 3.657 13.160 1.000 24.91 ATOM 2576 CB LEU B 111 80.522 2.369 13.980 1.000 26.44 ATOM 2577 CG LEU B 111 81.139 2.383 15.380 1.000 28.05 ATOM 2578 CD1 LEU B 111 80.668 3.604 16.161 1.000 25.21 ATOM 2579 CD2 LEU B 111 80.814 1.095 16.125 1.000 26.81 ATOM 2580 C LEU B 111 82.042 4.029 12.833 1.000 27.53 ATOM 2581 O LEU B 111 82.637 4.954 13.393 1.000 29.42 ATOM 2582 N GLU B 112 82.657 3.312 11.891 1.000 28.47 ATOM 2583 CA GLU B 112 84.097 3.523 11.692 1.000 32.01 ATOM 2584 CB GLU B 112 84.712 2.374 10.892 1.000 43.42 ATOM 2585 CG GLU B 112 85.202 1.218 11.745 1.000 58.71 ATOM 2586 CD GLU B 112 85.624 1.561 13.157 1.000 63.11 ATOM 2587 OE1 GLU B 112 86.853 1.662 13.402 1.000 56.52 ATOM 2588 OE2 GLU B 112 84.754 1.705 14.048 1.000 38.29 ATOM 2589 C GLU B 112 84.390 4.852 11.019 1.000 29.92 ATOM 2590 O GLU B 112 85.499 5.371 11.177 1.000 27.14 ATOM 2591 N ASP B 113 83.435 5.432 10.287 1.000 26.76 ATOM 2592 CA ASP B 113 83.634 6.806 9.832 1.000 23.28 ATOM 2593 CB ASP B 113 82.472 7.267 8.962 1.000 28.04 ATOM 2594 CG ASP B 113 82.718 7.128 7.474 1.000 31.68 ATOM 2595 OD1 ASP B 113 83.873 6.857 7.094 1.000 28.93 ATOM 2596 OD2 ASP B 113 81.748 7.292 6.704 1.000 29.11 ATOM 2597 C ASP B 113 83.774 7.745 11.033 1.000 23.71 ATOM 2598 O ASP B 113 84.565 8.688 11.039 1.000 25.19 ATOM 2599 N PHE B 114 82.981 7.481 12.078 1.000 23.64 ATOM 2600 CA PHE B 114 83.043 8.327 13.273 1.000 21.55 ATOM 2601 CB PHE B 114 81.856 8.044 14.192 1.000 21.55 ATOM 2602 CG PHE B 114 81.712 9.022 15.346 1.000 22.74 ATOM 2603 CD1 PHE B 114 82.303 8.752 16.571 1.000 24.12 ATOM 2604 CD2 PHE B 114 81.001 10.198 15.187 1.000 21.84 ATOM 2605 CE1 PHE B 114 82.174 9.637 17.625 1.000 23.11 ATOM 2606 CE2 PHE B 114 80.850 11.083 16.242 1.000 23.72 ATOM 2607 CZ PHE B 114 81.447 10.803 17.458 1.000 21.35 ATOM 2608 C PHE B 114 84.352 8.104 14.023 1.000 21.77 ATOM 2609 O PHE B 114 85.004 9.058 14.449 1.000 24.80 ATOM 2610 N GLN B 115 84.716 6.839 14.183 1.000 23.92 ATOM 2611 CA GLN B 115 85.919 6.434 14.898 1.000 26.72 ATOM 2612 CB GLN B 115 86.002 4.908 14.970 1.000 28.07 ATOM 2613 CG GLN B 115 87.126 4.379 15.851 1.000 29.18 ATOM 2614 CD GLN B 115 86.740 4.463 17.320 1.000 33.93 ATOM 2615 OE1 GLN B 115 8S.710 3.920 17.730 1.000 36.31 ATOM 2616 NE2 GLN B 115 87.560 5.151 18.103 1.000 31.38 ATOM 2617 C GLN B 115 87.182 6.977 14.242 1.000 25.49 ATOM 2618 O GLN B 115 88.089 7.449 14.921 1.000 26.49 ATOM 2619 N ARG B 116 87.244 6.906 12.918 1.000 22.33 ATOM 2620 CA ARG B 116 88.433 7.339 12.188 1.000 24.36 ATOM 2621 CB ARG B 116 88.272 7.028 10.700 1.000 22.95 ATOM 2622 C ARG B 116 88.723 8.818 12.389 1.000 21.93 ATOM 2623 O ARG B 116 89.868 9.240 12.574 1.000 22.76 ATOM 2624 N VAL B 117 87.675 9.638 12.347 1.000 22.20 ATOM 2625 CA VAL B 117 87.852 11.084 12.441 1.000 20.72 ATOM 2626 CB VAL B 117 86.580 11.816 11.993 1.000 20.31 ATOM 2627 CG1 VAL B 117 86.640 13.287 12.349 1.000 20.26 ATOM 2628 CG2 VAL B 117 86.392 11.669 10.484 1.000 27.13 ATOM 2629 C VAL B 117 88.249 11.483 13.857 1.000 23.41 ATOM 2630 O VAL B 117 89.115 12.336 14.039 1.000 26.63 ATOM 2631 N LEU B 118 87.637 10.854 14.853 1.000 19.32 ATOM 2632 CA LEU B 118 88.020 10.966 16.248 1.000 23.34 ATOM 2633 CB LEU B 118 87.227 10.034 17.158 1.000 24.15 ATOM 2634 CG LEU B 118 85.754 10.307 17.433 1.000 36.11 ATOM 2635 CD1 LEU B 118 85.303 9.517 18.654 1.000 34.48 ATOM 2636 CD2 LEU B 118 85.495 11.793 17.617 1.000 37.25 ATOM 2637 C LEU B 118 89.497 10.591 16.424 1.000 21.18 ATOM 2638 O LEU B 118 90.305 11.315 16.996 1.000 24.74 ATOM 2639 N ASP B 119 89.826 9.409 15.907 1.000 19.51 ATOM 2640 CA ASP B 119 91.175 8.870 16.015 1.000 23.80 ATOM 2641 CB ASP B 119 91.255 7.538 15.259 1.000 22.73 ATOM 2642 CG ASP B 119 90.734 6.387 16.102 1.000 27.64 ATOM 2643 OD1 ASP B 119 90.874 5.229 15.655 1.000 38.04 ATOM 2644 OD2 ASP B 119 90.193 6.626 17.203 1.000 27.24 ATOM 2645 C ASP B 119 92.228 9.840 15.501 1.000 27.92 ATOM 2646 O ASP B 119 93.197 10.162 16.197 1.000 24.30 ATOM 2647 N VAL B 120 92.072 10.333 14.271 1.000 24.11 ATOM 2648 CA VAL B 120 93.094 11.250 13.774 1.000 21.70 ATOM 2649 CB VAL B 120 92.997 11.468 12.247 1.000 21.17 ATOM 2650 CG1 VAL B 120 94.025 12.498 11.801 1.000 19.78 ATOM 2651 CG2 VAL B 120 93.201 10.156 11.502 1.000 25.36 ATOM 2652 C VAL B 120 93.021 12.609 14.455 1.000 18.60 ATOM 2653 O VAL B 120 94.034 13.143 14.901 1.000 18.90 ATOM 2654 N ASN B 121 91.827 13.197 14.510 1.000 16.99 ATOM 2655 CA ASN B 121 91.699 14.592 14.914 1.000 19.35 ATOM 2656 CB ASN B 121 90.306 15.127 14.534 1.000 23.26 ATOM 2657 CG ASN B 121 90.183 15.419 13.051 1.000 26.22 ATOM 2658 OD1 ASN B 121 91.063 15.040 12.278 1.000 26.76 ATOM 2659 ND2 ASN B 121 89.110 16.088 12.650 1.000 19.20 ATOM 2660 C ASN B 121 91.894 14.825 16.409 1.000 19.21 ATOM 2661 O ASN B 121 92.515 15.818 16.774 1.000 21.98 ATOM 2662 N LEU B 122 91.341 13.944 17.232 1.000 20.95 ATOM 2663 CA LEU B 122 91.306 14.176 18.679 1.000 19.05 ATOM 2664 CB LEU B 122 89.905 13.857 19.189 1.000 18.59 ATOM 2665 CG LEU B 122 89.615 14.033 20.679 1.000 20.96 ATOM 2666 CD1 LEU B 122 90.069 15.391 21.190 1.000 16.90 ATOM 2667 CD2 LEU B 122 88.126 13.860 20.945 1.000 18.18 ATOM 2668 C LEU B 122 92.376 13.350 19.377 1.000 20.58 ATOM 2669 O LEU B 122 93.297 13.880 19.999 1.000 24.53 ATOM 2670 N MET B 123 92.291 12.025 19.278 1.000 19.48 ATOM 2671 CA MET B 123 93.308 11.158 19.874 1.000 22.29 ATOM 2672 CB MET B 123 92.982 9.693 19.590 1.000 22.09 ATOM 2673 CG MET B 123 93.957 8.703 20.207 1.000 23.89 ATOM 2674 SD MET B 123 95.361 8.365 19.122 1.000 29.30 ATOM 2675 CE MET B 123 94.591 7.184 18.008 1.000 26.18 ATOM 2676 C MET B 123 94.699 11.513 19.363 1.000 26.09 ATOM 2677 O MET B 123 95.641 11.661 20.142 1.000 23.77 ATOM 2678 N GLY B 124 94.829 11.663 18.043 1.000 22.76 ATOM 2679 CA GLY B 124 96.103 11.989 17.421 1.000 23.30 ATOM 2680 C GLY B 124 96.716 13.248 17.998 1.000 26.58 ATOM 2681 O GLY B 124 97.890 13.317 18.355 1.000 22.97 ATOM 2682 N THR B 125 95.907 14.299 18.113 1.000 20.71 ATOM 2683 CA THR B 125 96.370 15.521 18.762 1.000 18.75 ATOM 2684 CB THR B 125 95.285 16.611 18.685 1.000 22.80 ATOM 2685 OG1 THR B 125 95.241 17.153 17.356 1.000 23.16 ATOM 2686 CG2 THR B 125 95.604 17.748 19.648 1.000 15.94 ATOM 2687 C THR B 125 96.743 15.265 20.215 1.000 20.63 ATOM 2688 O THR B 125 97.778 15.746 20.683 1.000 23.52 ATOM 2689 N PHE B 126 95.948 14.514 20.983 1.000 20.41 ATOM 2690 CA PHE B 126 96.358 14.272 22.375 1.000 23.20 ATOM 2691 CB PHE B 126 95.263 13.545 23.158 1.000 19.10 ATOM 2692 CG PHE B 126 95.639 13.311 24.616 1.000 25.87 ATOM 2693 CD1 PHE B 126 95.581 14.353 25.523 1.000 22.37 ATOM 2694 CD2 PHE B 126 96.050 12.061 25.050 1.000 26.96 ATOM 2695 CE1 PHE B 126 95.935 14.154 26.850 1.000 22.65 ATOM 2696 CE2 PHE B 126 96.399 11.852 26.375 1.000 23.20 ATOM 2697 CZ PHE B 126 96.343 12.899 27.274 1.000 20.92 ATOM 2698 C PHE B 126 97.661 13.478 22.450 1.000 21.16 ATOM 2699 O PHE B 126 98.532 13.733 23.282 1.000 22.13 ATOM 2700 N ASN B 127 97.825 12.497 21.575 1.000 20.29 ATOM 2701 CA ASN B 127 99.040 11.690 21.502 1.000 22.57 ATOM 2702 CE ASN B 127 98.922 10.706 20.339 1.000 22.19 ATOM 2703 CG ASN B 127 99.979 9.621 20.359 1.000 28.15 ATOM 2704 OD1 ASN B 127 100.400 9.142 21.411 1.000 27.23 ATOM 2705 ND2 ASN B 127 100.399 9.231 19.159 1.000 23.88 ATOM 2706 C ASN B 127 100.287 12.547 21.334 1.000 26.24 ATOM 2707 O ASN B 127 101.293 12.353 22.021 1.000 27.74 ATOM 2708 N VAL B 128 100.239 13.509 20.412 1.000 21.97 ATOM 2709 CA VAL B 128 101.374 14.412 20.233 1.000 21.97 ATOM 2710 CE VAL B 128 101.182 15.276 18.969 1.000 25.49 ATOM 2711 CG1 VAL B 128 102.234 16.367 18.881 1.000 18.12 ATOM 2712 CG2 VAL B 128 101.212 14.383 17.730 1.000 21.07 ATOM 2713 C VAL B 128 101.571 15.300 21.454 1.000 24.63 ATOM 2714 O VAL B 128 102.697 15.551 21.878 1.000 24.16 ATOM 2715 N ILE B 129 100.482 15.802 22.040 1.000 21.34 ATOM 2716 CA ILE B 129 100.595 16.670 23.210 1.000 21.04 ATOM 2717 CE ILE B 129 99.207 17.164 23.671 1.000 21.80 ATOM 2718 CG2 ILE B 129 99.282 17.704 25.093 1.000 15.16 ATOM 2719 CG1 ILE B 129 98.559 18.184 22.731 1.000 19.30 ATOM 2720 CD1 ILE B 129 97.089 18.395 23.009 1.000 20.24 ATOM 2721 C ILE B 129 101.259 15.977 24.395 1.000 21.07 ATOM 2722 O ILE B 129 102.160 16.538 25.019 1.000 24.73 ATOM 2723 N ARG B 130 100.821 14.766 24.722 1.000 22.23 ATOM 2724 CA ARG B 130 101.320 14.074 25.907 1.000 23.38 ATOM 2725 CE ARG B 130 100.465 12.830 26.183 1.000 21.66 ATOM 2726 CG ARG B 130 100.867 11.603 25.400 1.000 20.29 ATOM 2727 CD ARG B 130 99.789 10.542 25.265 1.000 18.80 ATOM 2728 NE ARG B 130 100.255 9.485 24.364 1.000 22.82 ATOM 2729 CZ ARG B 130 101.032 8.465 24.704 1.000 28.05 ATOM 2730 NE1 ARG B 130 101.403 7.563 23.800 1.000 23.90 ATOM 2731 NE2 ARG B 130 101.461 8.305 25.951 1.000 20.66 ATOM 2732 C ARG B 130 102.791 13.701 25.769 1.000 29.73 ATOM 2733 O ARG B 130 103.571 13.761 26.724 1.000 23.87 ATOM 2734 N LEU B 131 103.193 13.303 24.568 1.000 27.25 ATOM 2735 CA LEU B 131 104.565 12.913 24.278 1.000 25.57 ATOM 2736 CB LEU B 131 104.620 12.045 23.019 1.000 26.19 ATOM 2737 CG LEU B 131 103.911 10.689 23.075 1.000 28.61 ATOM 2738 CD1 LEU B 131 103.958 9.978 21.721 1.000 23.83 ATOM 2739 CD2 LEU B 131 104.513 9.786 24.142 1.000 31.07 ATOM 2740 C LEU B 131 105.445 14.145 24.144 1.000 26.19 ATOM 2741 O LEU B 131 106.565 14.195 24.663 1.000 25.39 ATOM 2742 N VAL B 132 104.963 15.186 23.466 1.000 21.11 ATOM 2743 CA VAL B 132 105.780 16.391 23.341 1.000 17.60 ATOM 2744 CB VAL B 132 105.279 17.364 22.261 1.000 22.25 ATOM 2745 CG1 VAL B 132 104.101 18.197 22.728 1.000 23.13 ATOM 2746 CG2 VAL B 132 106.413 18.301 21.850 1.000 24.17 ATOM 2747 C VAL B 132 105.874 17.116 24.680 1.000 23.10 ATOM 2748 O VAL B 132 106.892 17.766 24.950 1.000 25.24 ATOM 2749 N ALA B 133 104.857 17.013 25.537 1.000 20.04 ATOM 2750 CA ALA B 133 104.985 17.654 26.852 1.000 22.03 ATOM 2751 CB ALA B 133 103.694 17.515 27.645 1.000 19.47 ATOM 2752 C ALA B 133 106.160 17.075 27.631 1.000 21.84 ATOM 2753 O ALA B 133 106.872 17.783 28.342 1.000 23.39 ATOM 2754 N GLY B 134 106.368 15.771 27.498 1.000 24.23 ATOM 2755 CA GLY B 134 107.452 15.085 28.179 1.000 31.61 ATOM 2756 C GLY B 134 108.812 15.508 27.658 1.000 34.00 ATOM 2757 O GLY B 134 109.784 15.551 28.414 1.000 29.77 ATOM 2758 N GLU B 135 108.886 15.826 26.367 1.000 33.32 ATOM 2759 CA GLU B 135 110.100 16.386 25.792 1.000 28.56 ATOM 2760 CB GLU B 135 110.039 16.427 24.262 1.000 27.20 ATOM 2761 CG GLU B 135 109.843 15.075 23.597 1.000 28.76 ATOM 2762 CD GLU B 135 111.100 14.232 23.700 1.000 35.06 ATOM 2763 OE1 GLU B 135 110.992 13.012 23.929 1.000 47.85 ATOM 2764 OE2 GLU B135 112.204 14.795 23.561 1.000 44.39 ATOM 2765 C GLU B 135 110.324 17.805 26.301 1.000 27.32 ATOM 2766 O GLU B 135 111.437 18.185 26.662 1.000 26.88 ATOM 2767 N MET B 136 109.245 18.602 26.317 1.000 22.38 ATOM 2768 CA MET B 136 109.416 19.995 26.725 1.000 22.02 ATOM 2769 CB MET B 136 108.151 20.800 26.448 1.000 23.97 ATOM 2770 CG MET B 136 107.833 21.067 24.990 1.000 28.51 ATOM 2771 SD MET B 136 106.121 21.622 24.802 1.000 26.00 ATOM 2772 CE MET B 136 106.071 22.029 23.057 1.000 22.80 ATOM 2773 C MET B 136 109.767 20.084 28.205 1.000 20.95 ATOM 2774 O MET B 136 110.397 21.035 28.665 1.000 27.02 ATOM 2775 N GLY B 137 109.343 19.092 28.983 1.000 23.73 ATOM 2776 CA GLY B 137 109.638 19.135 30.413 1.000 30.04 ATOM 2777 C GLY B 137 111.125 19.064 30.698 1.000 32.99 ATOM 2778 O GLY B 137 111.555 19.376 31.812 1.000 33.93 ATOM 2779 N GLN B 138 111.925 18.658 29.718 1.000 29.39 ATOM 2780 CA GLN B 138 113.375 18.581 29.892 1.000 28.86 ATOM 2781 CB GLN B 138 113.963 17.515 28.976 1.000 34.26 ATOM 2782 C GLN B 138 114.033 19.924 29.635 1.000 31.61 ATOM 2783 O GLN B 138 115.205 20.149 29.939 1.000 33.07 ATOM 2784 N ASN B 139 113.297 20.877 29.059 1.000 30.51 ATOM 2785 CA ASN B 139 113.904 22.175 28.786 1.000 29.96 ATOM 2786 CB ASN B 139 113.033 22.995 27.840 1.000 31.82 ATOM 2787 CG ASN B 139 112.839 22.378 26.470 1.000 37.24 ATOM 2788 OD1 ASN B 139 113.667 21.614 25.973 1.000 30.68 ATOM 2789 ND2 ASN B 139 111.710 22.731 25.850 1.000 28.36 ATOM 2790 C ASN B 139 114.095 22.959 30.076 1.000 34.50 ATOM 2791 O ASN B 139 113.248 22.886 30.972 1.000 32.01 ATOM 2792 N GLU B 140 115.187 23.712 30.169 1.000 31.95 ATOM 2793 CA GLU B 140 115.309 24.671 31.263 1.000 32.60 ATOM 2794 CB GLU B 140 116.719 25.220 31.373 1.000 36.62 ATOM 2795 C GLU B 140 114.304 25.799 31.033 1.000 31.18 ATOM 2796 O GLU B 140 114.197 26.259 29.896 1.000 28.53 ATOM 2797 N PRO B 141 113.584 26.229 32.058 1.000 31.88 ATOM 2798 CD PRO B 141 113.641 25.759 33.456 1.000 30.29 ATOM 2799 CA PRO B 141 112.590 27.290 31.875 1.000 31.37 ATOM 2800 CB PRO B 141 112.002 27.495 33.271 1.000 32.31 ATOM 2801 CG PRO B 141 112.345 26.259 34.028 1.000 30.62 ATOM 2802 C PRO B 141 113.257 28.576 31.408 1.000 36.56 ATOM 2803 O PRO B 141 114.386 28.849 31.811 1.000 38.29 ATOM 2804 N ASP B 142 112.578 29.361 30.577 1.000 32.11 ATOM 2805 CA ASP B 142 113.190 30.602 30.108 1.000 29.02 ATOM 2806 CB ASP B 142 112.523 31.107 28.835 1.000 34.13 ATOM 2807 CG ASP B 142 111.042 31.388 28.975 1.000 35.91 ATOM 2808 OD1 ASP B 142 110.540 31.478 30.114 1.000 27.63 ATOM 2809 OD2 ASP B 142 110.383 31.505 27.919 1.000 36.65 ATOM 2810 C ASP B 142 113.113 31.659 31.199 1.000 35.02 ATOM 2811 O ASP B 142 112.733 31.348 32.329 1.000 34.17 ATOM 2812 N GLN B 143 113.459 32.893 30.853 1.000 35.14 ATOM 2813 CA GLN B 143 113.391 34.002 31.801 1.000 37.94 ATOM 2814 CB GLN B 143 113.878 35.288 31.147 1.000 37.47 ATOM 2815 C GLN B 143 111.979 34.184 32.344 1.000 39.06 ATOM 2816 O GLN B 143 111.781 34.729 33.431 1.000 37.62 ATOM 2817 N GLY B 144 110.979 33.726 31.593 1.000 33.77 ATOM 2818 CA GLY B 144 109.590 33.862 32.005 1.000 29.37 ATOM 2819 C GLY B 144 109.113 32.632 32.746 1.000 29.22 ATOM 2820 O GLY B 144 107.965 32.517 33.166 1.000 31.92 ATOM 2821 N GLY B 145 110.023 31.673 32.916 1.000 28.73 ATOM 2822 CA GLY B 145 109.679 30.408 33.540 1.000 27.23 ATOM 2823 C GLY B 145 109.010 29.468 32.550 1.000 28.54 ATOM 2824 O GLY B 145 108.404 28.469 32.947 1.000 26.30 ATOM 2825 N GLN B 146 109.115 29.772 31.257 1.000 26.91 ATOM 2826 CA GLN B 146 108.395 28.963 30.274 1.000 27.98 ATOM 2827 CB GLN B 146 107.862 29.872 29.154 1.000 24.94 ATOM 2828 CG GLN B 146 106.886 29.135 28.247 1.000 32.11 ATOM 2829 CD GLN B 146 106.239 30.065 27.238 1.000 27.79 ATOM 2830 OE1 GLN B 146 105.335 30.822 27.576 1.000 24.50 ATOM 2831 NE2 GLN B 146 106.727 29.988 26.002 1.000 27.50 ATOM 2832 C GLN B 146 109.243 27.863 29.657 1.000 26.64 ATOM 2833 O GLN B 146 110.385 28.076 29.246 1.000 27.40 ATOM 2834 N ARG B 147 108.680 26.659 29.551 1.000 20.15 ATOM 2835 CA ARG B 147 109.392 25.561 28.913 1.000 21.33 ATOM 2836 CB ARG B 147 109.340 24.300 29.782 1.000 22.83 ATOM 2837 CG ARG B 147 110.180 24.362 31.062 1.000 22.46 ATOM 2838 CD ARG B 147 110.143 22.991 31.707 1.000 25.58 ATOM 2839 NE ARG B 147 111.072 22.800 32.805 1.000 26.67 ATOM 2840 CZ ARG B 147 110.759 22.976 34.080 1.000 32.90 ATOM 2841 NH1 ARG B 147 111.670 22.773 35.023 1.000 35.72 ATOM 2842 NH2 ARG B 147 109.528 23.358 34.404 1.000 28.27 ATOM 2843 C ARG B 147 108.820 25.211 27.544 1.000 29.41 ATOM 2844 O ARG B 147 109.465 24.482 26.784 1.000 24.64 ATOM 2845 N GLY B 148 107.613 25.681 27.214 1.000 26.59 ATOM 2846 CA GLY B 148 107.026 25.263 25.945 1.000 23.20 ATOM 2847 C GLY B 148 105.685 25.932 25.685 1.000 28.53 ATOM 2848 O GLY B 148 105.068 26.467 26.610 1.000 20.78 ATOM 2849 N VAL B 149 105.245 25.895 24.434 1.000 24.83 ATOM 2850 CA VAL B 149 103.944 26.359 23.980 1.000 22.50 ATOM 2851 CB VAL B 149 104.009 27.711 23.253 1.000 22.87 ATOM 2852 CG1 VAL B 149 102.597 28.262 23.025 1.000 25.59 ATOM 2853 CG2 VAL B 149 104.853 28.720 24.007 1.000 28.65 ATOM 2854 C VAL B 149 103.335 25.328 23.027 1.000 24.60 ATOM 28S5 O VAL B 149 103.985 24.928 22.062 1.000 21.79 ATOM 2856 N ILE B 150 102.115 24.886 23.299 1.000 22.21 ATOM 2857 CA ILE B 150 101.412 23.931 22.457 1.000 22.43 ATOM 2858 CB ILE B 150 101.063 22.642 23.214 1.000 24.72 ATOM 2859 CG2 ILE B 150 100.208 21.687 22.386 1.000 19.63 ATOM 2860 CD1 ILE B 150 102.294 21.896 23.756 1.000 21.59 ATOM 2861 CD1 ILE B 150 101.918 20.680 24.581 1.000 23.41 ATOM 2862 C ILE B 150 100.145 24.584 21.898 1.000 24.76 ATOM 2863 O ILE B 150 99.353 25.137 22.662 1.000 21.45 ATOM 2864 N ILE B 151 99.976 24.53 220.581 1.000 22.74 ATOM 2865 CA ILE B 151 98.836 25.139 19.898 1.000 18.41 ATOM 2866 CB ILE B 151 99.262 26.272 18.954 1.000 20.13 ATOM 2867 CG2 ILE B 151 98.063 27.005 18.358 1.000 13.13 ATOM 2868 CG1 ILE B 151 100.225 27.281 19.595 1.000 23.87 ATOM 2869 CD1 ILE B 151 100.757 28.306 18.615 1.000 27.17 ATOM 2870 C ILE B 151 98.090 24.068 19.118 1.000 20.55 ATOM 2871 O ILE B 151 98.702 23.387 18.295 1.000 22.75 ATOM 2872 N ASN B 152 96.800 23.922 19.383 1.000 20.72 ATOM 2873 CA ASN B 152 95.978 22.934 18.701 1.000 18.58 ATOM 2874 CB ASN B 152 95.082 22.197 19.702 1.000 18.64 ATOM 2875 CG ASN B 152 95.890 21.725 20.896 1.000 22.42 ATOM 2876 OD1 ASN B 152 95.586 22.026 22.051 1.000 31.28 ATOM 2877 ND2 ASN B 152 96.954 20.977 20.642 1.000 15.90 ATOM 2878 C ASN B 152 95.116 23.588 17.627 1.000 21.08 ATOM 2879 O ASN B 152 94.934 24.805 17.623 1.000 20.68 ATOM 2880 N THR B 153 94.584 22.782 16.721 1.000 20.37 ATOM 2881 CA THR B 153 93.670 23.303 15.706 1.000 21.06 ATOM 2882 CB THR B 153 94.149 23.034 14.273 1.000 21.72 ATOM 2883 OG1 THR B 153 95.481 23.558 14.123 1.000 20.20 ATOM 2884 CG2 THR B 153 93.262 23.760 13.272 1.000 18.62 ATOM 2885 C THR B 153 92.299 22.668 15.923 1.000 19.15 ATOM 2886 O THR B 153 92.150 21.460 15.761 1.000 21.82 ATOM 2887 N ALA B 154 91.337 23.499 16.317 1.000 17.65 ATOM 2888 CA ALA B 154 89.967 23.002 16.451 1.000 22.08 ATOM 2889 CB ALA B 154 89.255 23.587 17.656 1.000 19.39 ATOM 2890 C ALA B 154 89.252 23.339 15.138 1.000 21.89 ATOM 2891 O ALA B 154 89.788 22.995 14.076 1.000 21.95 ATOM 2892 N SER B 155 88.113 24.003 15.248 1.000 19.65 ATOM 2893 CA SER B 155 87.331 24.459 14.112 1.000 19.95 ATOM 2894 CB SER B 155 86.953 23.281 13.212 1.000 19.33 ATOM 2895 OG SER B 155 85.898 23.638 12.326 1.000 20.16 ATOM 2896 CB SER B 155 86.071 25.161 14.598 1.000 20.44 ATOM 2897 O SER B 155 85.582 24.855 15.684 1.000 19.66 ATOM 2898 N VAL B 156 85.494 26.082 13.832 1.000 16.22 ATOM 2899 CA VAL B 156 84.216 26.649 14.282 1.000 16.46 ATOM 2900 CB VAL B 156 83.758 27.804 13.390 1.000 22.77 ATOM 2901 CG1 VAL B 156 84.736 28.970 13.469 1.000 23.36 ATOM 2902 CG2 VAL B 156 83.614 27.320 11.952 1.000 25.09 ATOM 2903 C VAL B 156 83.130 25.577 14.345 1.000 19.15 ATOM 2904 O VAL B 156 82.119 25.778 15.042 1.000 21.77 ATOM 2905 N ALA B 157 83.315 24.438 13.682 1.000 17.00 ATOM 2906 CA ALA B 157 82.380 23.321 13.744 1.000 17.11 ATOM 2907 CB ALA B 157 82.779 22.211 12.782 1.000 13.23 ATOM 2908 C ALA B 157 82.250 22.758 15.157 1.000 22.42 ATOM 2909 O ALA B 157 81.307 22.027 15.471 1.000 24.11 ATOM 2910 N ALA B 158 83.190 23.098 16.028 1.000 22.00 ATOM 2911 CA ALA B 158 83.094 22.828 17.447 1.000 22.62 ATOM 2912 CB ALA B 158 84.350 23.302 18.173 1.000 19.72 ATOM 2913 C ALA B 158 81.882 23.544 18.043 1.000 23.87 ATOM 2914 O ALA B 158 81.312 23.092 19.036 1.000 23.62 ATOM 2915 N PHE B 159 81.514 24.670 17.437 1.000 21.51 ATOM 2916 CA PHE B 159 80.464 25.527 17.981 1.000 22.39 ATOM 2917 CB PHE B 159 81.035 26.942 18.156 1.000 21.64 ATOM 2918 CG PHE B 159 82.255 26.961 19.067 1.000 24.89 ATOM 2919 CD1 PHE B 159 83.487 27.354 18.565 1.000 23.04 ATOM 2920 CD2 PHE B 159 82.143 26.589 20.397 1.000 24.09 ATOM 2921 CE1 PHE B 159 84.599 27.372 19.393 1.000 24.68 ATOM 2922 CE2 PHE B 159 83.250 26.603 21.229 1.000 24.96 ATOM 2923 CZ PHE B 159 84.473 26.994 20.721 1.000 22.41 ATOM 2924 C PHE B 159 79.200 25.585 17.133 1.000 25.85 ATOM 2925 O PHE B 159 78.100 25.721 17.687 1.000 21.57 ATOM 2926 N GLU B 160 79.327 25.497 15.813 1.000 22.51 ATOM 2927 CA GLU B 160 78.181 25.504 14.910 1.000 23.96 ATOM 2928 CB GLU B 160 78.041 26.820 14.150 1.000 26.01 ATOM 2929 CG GLU B 160 77.979 28.098 14.948 1.000 32.94 ATOM 2930 CD GLU B 160 79.247 28.924 14.932 1.000 33.82 ATOM 2931 OE1 GLU B 160 79.637 29.411 16.013 1.000 28.19 ATOM 2932 OE2 GLU B 160 79.877 29.109 13.866 1.000 27.13 ATOM 2933 C GLU B 160 78.309 24.378 13.880 1.000 22.36 ATOM 2934 O GLU B 160 78.302 24.652 12.675 1.000 26.67 ATOM 2935 N GLY B 161 78.442 23.144 14.329 1.000 18.77 ATOM 2936 CA GLY B 161 78.615 22.033 13.392 1.000 22.85 ATOM 2937 C GLY B 161 77.447 22.008 12.412 1.000 25.07 ATOM 2938 O GLY B 161 76.305 22.215 12.818 1.000 20.77 ATOM 2939 N GLN B 162 77.735 21.776 11.142 1.000 23.20 ATOM 2940 CA GLN B 162 76.717 21.802 10.100 1.000 25.68 ATOM 2941 CB GLN B 162 77.327 22.268 8.772 1.000 21.32 ATOM 2942 CG GLN B 162 78.011 23.621 8.830 1.000 22.80 ATOM 2943 CD GLN B 162 78.260 24.186 7.447 1.000 26.50 ATOM 2944 OE1 GLN B 162 79.170 23.717 6.765 1.000 30.69 ATOM 2945 NE2 GLN B 162 77.474 25.170 7.034 1.000 19.53 ATOM 2946 C GLN B 162 76.097 20.430 9.898 1.000 23.24 ATOM 2947 O GLN B 162 76.613 19.436 10.411 1.000 23.86 ATOM 2948 N VAL B 163 75.010 20.370 9.133 1.000 23.04 ATOM 2949 CA VAL B 163 74.513 19.067 8.695 1.000 23.64 ATOM 2950 CB VAL B 163 73.359 19.190 7.685 1.000 21.10 ATOM 2951 CG1 VAL B 163 73.011 17.821 7.112 1.000 24.07 ATOM 2952 CG2 VAL B 163 72.124 19.807 8.331 1.000 18.88 ATOM 2953 C VAL B 163 75.656 18.277 8.048 1.000 25.39 ATOM 2954 O VAL B 163 76.390 18.822 7.216 1.000 28.18 ATOM 2955 N GLY B 164 75.804 17.016 8.423 1.000 24.05 ATOM 2956 CA GLY B 164 76.838 16.139 7.902 1.000 22.74 ATOM 2957 C GLY B 164 78.105 16.104 8.741 1.000 25.15 ATOM 2958 O GLY B 164 78.930 15.201 8.552 1.000 25.10 ATOM 2959 N GLN B 165 78.283 17.062 9.643 1.000 22.51 ATOM 2960 CA GLN B 165 79.519 17.249 10.387 1.000 24.93 ATOM 2961 CB GLN B 165 79.788 18.752 10.551 1.000 23.90 ATOM 2962 CG GLN B 165 80.258 19.481 9.310 1.000 30.10 ATOM 2963 CD GLN B 165 80.846 20.839 9.652 1.000 31.96 ATOM 2964 OE1 GLN B 165 80.265 21.595 10.432 1.000 28.58 ATOM 2965 NE2 GLN B 165 82.002 21.157 9.072 1.000 32.65 ATOM 2966 C GLN B 165 79.551 16.655 11.789 1.000 23.68 ATOM 2967 O GLN B 165 80.385 17.071 12.594 1.000 24.30 ATOM 2968 N ALA B 166 78.686 15.714 12.126 1.000 21.51 ATOM 2969 CA ALA B 166 78.662 15.164 13.481 1.000 20.54 ATOM 2970 CB ALA B 166 77.593 14.089 13.571 1.000 18.83 ATOM 2971 C ALA B 166 80.014 14.619 13.924 1.000 25.40 ATOM 2972 O ALA B 166 80.485 14.947 15.018 1.000 25.59 ATOM 2973 N ALA B 167 80.685 13.787 13.132 1.000 23.03 ATOM 2974 CA ALA B 167 81.962 13.230 13.597 1.000 21.41 ATOM 2975 CB ALA B 167 82.413 12.108 12.678 1.000 21.78 ATOM 2976 C ALA B 167 83.041 14.294 13.736 1.000 22.03 ATOM 2977 O ALA B 167 83.735 14.367 14.758 1.000 24.57 ATOM 2978 N TYR B 168 83.200 15.138 12.732 1.000 16.78 ATOM 2979 CA TYR B 168 84.171 16.217 12.748 1.000 18.49 ATOM 2980 CB TYR B 168 84.094 17.005 11.444 1.000 20.42 ATOM 2981 CG TYR B 168 85.185 18.007 11.174 1.000 17.98 ATOM 2982 CD1 TYR B 168 86.463 17.607 10.803 1.000 21.16 ATOM 2983 CE1 TYR B 168 87.460 18.536 10.555 1.000 20.16 ATOM 2984 CD2 TYR B 168 84.942 19.370 11.282 1.000 17.16 ATOM 2985 CE2 TYR B 168 85.930 20.301 11.035 1.000 21.08 ATOM 2986 CZ TYR B 168 87.192 19.875 10.670 1.000 23.37 ATOM 2987 OB TYR B 168 88.163 20.821 10.429 1.000 24.37 ATOM 2988 C TYR B 168 83.921 17.154 13.927 1.000 24.27 ATOM 2989 O TYR B 168 84.858 17.511 14.641 1.000 20.90 ATOM 2990 N SER B 169 82.652 17.544 14.099 1.000 18.79 ATOM 2991 CA SER B 169 82.284 18.430 15.190 1.000 18.00 ATOM 2992 CB SER B 169 80.801 18.780 15.129 1.000 21.17 ATOM 2993 OG SER B 169 80.533 19.822 14.200 1.000 21.93 ATOM 2994 C SER B 169 82.627 17.795 16.537 1.000 23.23 ATOM 2995 O SER B 169 83.059 18.494 17.452 1.000 24.85 ATOM 2996 N ALA B 170 82.432 16.486 16.638 1.000 21.87 ATOM 2997 CA ALA B 170 82.720 15.772 17.875 1.000 21.87 ATOM 2998 CE ALA B 170 82.330 14.309 17.743 1.000 18.73 ATOM 2999 C ALA B 170 84.203 15.900 18.221 1.000 25.27 ATOM 3000 O ALA B 170 84.587 16.203 19.351 1.000 19.26 ATOM 3001 N SER B 171 85.004 15.648 17.185 1.000 19.22 ATOM 3002 CA SER B 171 86.454 15.647 17.335 1.000 19.66 ATOM 3003 CE SER B 171 87.128 15.093 16.073 1.000 18.82 ATOM 3004 OG SER B 171 87.134 16.064 15.033 1.000 21.75 ATOM 3005 C SER B 171 86.960 17.044 17.654 1.000 23.15 ATOM 3006 O SER B 171 87.856 17.202 18.489 1.000 24.32 ATOM 3007 N LYS B 172 86.395 18.073 17.009 1.000 20.33 ATOM 3008 CA LYS B 172 86.919 19.420 17.255 1.000 19.93 ATOM 3009 CE LYS B 172 86.592 20.350 16.084 1.000 17.49 ATOM 3010 CG LYS B 172 87.296 19.943 14.791 1.000 19.56 ATOM 3011 CD LYS B 172 88.807 19.836 14.962 1.000 20.06 ATOM 3012 CE LYS B 172 89.525 19.640 13.636 1.000 22.40 ATOM 3013 NZ LYS B 172 91.012 19.804 13.754 1.000 14.90 ATOM 3014 C LYS B 172 86.413 19.968 18.588 1.000 22.62 ATOM 3015 O LYS B 172 87.101 20.753 19.247 1.000 20.13 ATOM 3016 N GLY B 173 85.221 19.547 18.993 1.000 20.91 ATOM 3017 CA GLY B 173 84.689 19.941 20.296 1.000 18.93 ATOM 3018 C GLY B 173 85.520 19.315 21.406 1.000 20.82 ATOM 3019 O GLY B 173 85.720 19.940 22.447 1.000 24.27 ATOM 3020 N GLY B 174 86.005 18.106 21.175 1.000 18.50 ATOM 3021 CA GLY B 174 86.899 17.424 22.109 1.000 17.33 ATOM 3022 C GLY B 174 88.200 18.187 22.265 1.000 22.82 ATOM 3023 O GLY B 174 88.694 18.342 23.382 1.000 17.85 ATOM 3024 N ILE B 175 88.762 18.676 21.149 1.000 23.77 ATOM 3025 CA ILE B 175 89.953 19.506 21.251 1.000 18.10 ATOM 3026 CB ILE B 175 90.512 19.945 19.888 1.000 23.18 ATOM 3027 CG2 ILE B 175 91.745 20.818 20.126 1.000 14.17 ATOM 3028 CG1 ILE B 175 90.847 18.832 18.900 1.000 20.34 ATOM 3029 CD1 ILE B 175 92.017 17.985 19.344 1.000 28.39 ATOM 3030 C ILE B 175 89.667 20.770 22.057 1.000 19.76 ATOM 3031 O ILE B 175 90.452 21.171 22.919 1.000 21.09 ATOM 3032 N VAL B 176 88.537 21.418 21.770 1.000 13.27 ATOM 3033 CA VAL B 176 88.169 22.577 22.589 1.000 16.26 ATOM 3034 CB VAL B 176 86.848 23.209 22.129 1.000 20.98 ATOM 3035 CG1 VAL B 176 86.280 24.144 23.187 1.000 17.07 ATOM 3036 CG2 VAL B 176 87.045 23.961 20.813 1.000 19.89 ATOM 3037 C VAL B 176 88.069 22.181 24.066 1.000 18.42 ATOM 3038 O VAL B 176 88.643 22.846 24.932 1.000 19.91 ATOM 3039 N GLY B 177 87.352 21.108 24.367 1.000 18.87 ATOM 3040 CA GLY B 177 87.058 20.737 25.745 1.000 21.80 ATOM 3041 C GLY B 177 88.273 20.415 26.584 1.000 25.98 ATOM 3042 O GLY B 177 88.351 20.701 27.785 1.000 19.39 ATOM 3043 N MET B 178 89.275 19.784 25.961 1.000 20.82 ATOM 3044 CA MET B 178 90.460 19.398 26.718 1.000 18.94 ATOM 3045 CE MET B 178 91.065 18.115 26.138 1.000 20.57 ATOM 3046 CG MET B 178 91.703 18.285 24.763 1.000 20.96 ATOM 3047 SD MET B 178 92.375 16.749 24.092 1.000 24.89 ATOM 3048 CE MET B 178 93.471 17.405 22.833 1.000 17.24 ATOM 3049 C MET B 178 91.491 20.514 26.750 1.000 21.46 ATOM 3050 O MET B 178 92.536 20.344 27.390 1.000 22.19 ATOM 3051 N THR B 179 91.227 21.638 26.084 1.000 17.14 ATOM 3052 CA THR B 179 92.236 22.705 26.048 1.000 15.87 ATOM 3053 CB THR B 179 91.795 23.851 25.128 1.000 19.17 ATOM 3054 OG1 THR B 179 91.840 23.407 23.763 1.000 18.87 ATOM 3055 CG2 THR B 179 92.744 25.035 25.181 1.000 15.02 ATOM 3056 C THR B 179 92.555 23.238 27.439 1.000 24.29 ATOM 3057 O THR B 179 93.725 23.373 27.819 1.000 19.80 ATOM 3058 N LEU B 180 91.541 23.553 28.242 1.000 21.27 ATOM 3059 CA LEU B 180 91.803 24.095 29.574 1.000 19.96 ATOM 3060 CB LEU B 180 90.523 24.644 30.212 1.000 14.13 ATOM 3061 CG LEU B 180 90.683 25.218 31.623 1.000 23.37 ATOM 3062 CD1 LEU B 180 91.668 26.377 31.621 1.000 24.56 ATOM 3063 CD2 LEU B 180 89.332 25.648 32.181 1.000 23.02 ATOM 3064 C LEU B 180 92.424 23.078 30.525 1.000 18.79 ATOM 3065 O LEU B 180 93.438 23.415 31.163 1.000 24.04 ATOM 3066 N PRO B 181 91.861 21.889 30.685 1.000 18.00 ATOM 3067 CD PRO B 181 90.665 21.327 30.040 1.000 19.72 ATOM 3068 CA PRO B 181 92.454 20.940 31.646 1.000 19.59 ATOM 3069 CB PRO B 181 91.563 19.705 31.534 1.000 23.04 ATOM 3070 CG PRO B 181 90.850 19.848 30.226 1.000 20.73 ATOM 3071 C PRO B 181 93.896 20.594 31.292 1.000 27.33 ATOM 3072 O PRO B 181 94.739 20.409 32.174 1.000 20.10 ATOM 3073 N ILE B 182 94.220 20.508 29.996 1.000 19.63 ATOM 3074 CA ILE B 182 95.634 20.247 29.679 1.000 18.27 ATOM 3075 CB ILE B 182 95.813 19.877 28.200 1.000 20.42 ATOM 3076 CG2 ILE B 182 97.282 19.829 27.808 1.000 18.13 ATOM 3077 CG1 ILE B 182 95.125 18.561 27.833 1.000 17.30 ATOM 3078 CD1 ILE B 182 95.026 18.293 26.345 1.000 19.94 ATOM 3079 C ILE B 182 96.470 21.450 30.080 1.000 22.64 ATOM 3080 O ILE B 182 97.552 21.273 30.648 1.000 23.28 ATOM 3081 N ALA B 183 95.981 22.665 29.823 1.000 16.56 ATOM 3082 CA ALA B 183 96.716 23.844 30.270 1.000 17.31 ATOM 3083 CB ALA B 183 96.034 25.129 29.836 1.000 20.13 ATOM 3084 C ALA B 183 96.877 23.807 31.787 1.000 22.11 ATOM 3085 O ALA B 183 97.921 24.140 32.343 1.000 17.99 ATOM 3086 N ARG B 184 95.829 23.388 32.492 1.000 19.71 ATOM 3087 CA ARG B 184 95.925 23.319 33.956 1.000 22.24 ATOM 3088 CB ARG B 184 94.538 23.027 34.551 1.000 15.89 ATOM 3089 CG ARG B 184 93.616 24.229 34.372 1.000 15.80 ATOM 3090 CD ARG B 184 92.143 23.879 34.567 1.000 18.23 ATOM 3091 NE ARG B 184 91.434 25.074 35.063 1.000 23.39 ATOM 3092 CZ ARG B 184 90.228 25.034 35.628 1.000 21.65 ATOM 3093 NH1 ARG B 184 89.675 26.163 36.047 1.000 18.77 ATOM 3094 NH2 ARG B 184 89.596 23.878 35.757 1.000 17.16 ATOM 3095 C ARG B 184 96.971 22.287 34.361 1.000 19.92 ATOM 3096 O ARG B 184 97.823 22.537 35.216 1.000 18.04 ATOM 3097 N ASP B 185 96.925 21.123 33.718 1.000 15.09 ATOM 3098 CA ASP B 185 97.858 20.043 33.988 1.000 19.30 ATOM 3099 CB ASP B 185 97.691 18.914 32.979 1.000 22.62 ATOM 3100 CG ASP B 185 96.646 17.872 33.249 1.000 24.49 ATOM 3101 OD1 ASP B 185 96.474 17.005 32.354 1.000 20.08 ATOM 3102 OD2 ASP B 185 96.008 17.896 34.321 1.000 18.64 ATOM 3103 C ASP B 185 99.310 20.510 33.908 1.000 26.52 ATOM 3104 O ASP B 185 100.133 20.151 34.753 1.000 21.04 ATOM 3105 N LEU B 186 99.629 21.284 32.872 1.000 22.36 ATOM 3106 CA LEU B 186 101.027 21.590 32.551 1.000 23.22 ATOM 3107 CB LEU B 186 101.228 21.533 31.027 1.000 20.41 ATOM 3108 CG1 LEU B 186 100.941 20.172 30.391 1.000 22.94 ATOM 3109 CD1 LEU B 186 101.144 20.239 28.878 1.000 21.64 ATOM 3110 CD2 LEU B 186 101.818 19.106 31.038 1.000 17.63 ATOM 3111 C LEU B 186 101.481 22.946 33.058 1.000 22.22 ATOM 3112 O LEU B 186 102.652 23.319 32.973 1.000 25.41 ATOM 3113 N ALA B 187 100.555 23.729 33.595 1.000 13.92 ATOM 3114 CA ALA B 187 100.909 25.000 34.210 1.000 16.83 ATOM 3115 CB ALA B 187 99.648 25.573 34.846 1.000 17.97 ATOM 3116 C ALA B 187 102.045 24.894 35.219 1.000 23.80 ATOM 3117 O ALA B 187 102.964 25.737 35.187 1.000 21.12 ATOM 3118 N PRO B 188 102.088 23.933 36.134 1.000 25.14 ATOM 3119 CD PRO B 188 101.118 22.862 36.400 1.000 29.38 ATOM 3120 CA PRO B 188 103.226 23.871 37.065 1.000 28.38 ATOM 3121 CB PRO B 188 102.961 22.617 37.909 1.000 29.07 ATOM 3122 CG PRO B 188 101.522 22.300 37.721 1.000 30.89 ATOM 3123 C PRO B 188 104.566 23.693 36.364 1.000 33.56 ATOM 3124 O PRO B 188 105.626 23.900 36.966 1.000 28.73 ATOM 3125 N ILE B 189 104.572 23.295 35.085 1.000 27.67 ATOM 3126 CA ILE B 189 105.895 23.163 34.465 1.000 26.87 ATOM 3127 CB ILE B 189 106.105 21.739 33.932 1.000 30.74 ATOM 3128 CG2 ILE B 189 106.222 20.759 35.101 1.000 36.88 ATOM 3129 CD1 ILE B 189 105.044 21.259 32.943 1.000 26.76 ATOM 3130 CD1 ILE B 189 105.239 19.805 32.560 1.000 31.10 ATOM 3131 C ILE B 189 106.098 24.202 33.378 1.000 23.49 ATOM 3132 O ILE B 189 107.081 24.145 32.640 1.000 26.22 ATOM 3133 N GLY B 190 105.204 25.185 33.267 1.000 18.26 ATOM 3134 CA GLY B 190 105.447 26.271 32.329 1.000 18.80 ATOM 3135 C GLY B 190 105.210 25.913 30.880 1.000 23.71 ATOM 3136 O GLY B 190 105.895 26.420 29.978 1.000 25.00 ATOM 3137 N ILE B 191 104.230 25.044 30.606 1.000 17.78 ATOM 3138 CA ILE B 191 103.883 24.834 29.190 1.000 20.17 ATOM 3139 CB ILE B 191 104.015 23.354 28.822 1.000 18.88 ATOM 3140 CG2 ILE B 191 103.505 23.071 27.422 1.000 23.32 ATOM 3141 CG1 ILE B 191 105.456 22.821 28.991 1.000 18.18 ATOM 3142 CD1 ILE B 191 105.515 21.310 29.030 1.000 18.45 ATOM 3143 C ILE B 191 102.485 25.372 28.900 1.000 21.54 ATOM 3144 O ILE B 191 101.498 24.818 29.392 1.000 25.82 ATOM 3145 N ARG B 192 102.372 26.445 28.127 1.000 16.14 ATOM 3146 CA ARG B 192 101.081 27.041 27.803 1.000 19.05 ATOM 3147 CB ARG B 192 101.221 28.467 27.285 1.000 19.93 ATOM 3148 CG ARG B 192 101.763 29.513 28.236 1.000 19.68 ATOM 3149 CD ARG B 192 101.600 30.881 27.595 1.000 21.27 ATOM 3150 NE ARG B 192 102.670 31.168 26.636 1.000 22.16 ATOM 3151 CZ ARG B 192 102.485 31.544 25.382 1.000 22.96 ATOM 3152 NH1 ARG B 192 101.256 31.674 24.895 1.000 19.21 ATOM 3153 NH2 ARG B 192 103.537 31.784 24.605 1.000 21.25 ATOM 3154 C ARG B 192 100.361 26.239 26.723 1.000 19.37 ATOM 3155 O ARG B 192 101.027 25.680 25.848 1.000 24.14 ATOM 3156 N VAL B 193 99.040 26.191 26.788 1.000 20.05 ATOM 3157 CA VAL B 193 98.241 25.380 25.863 1.000 18.11 ATOM 3158 CB VAL B 193 97.685 24.114 26.518 1.000 20.36 ATOM 3159 CG1 VAL B 193 96.889 23.250 25.545 1.000 20.35 ATOM 3160 CG2 VAL B 193 98.814 23.273 27.113 1.000 16.91 ATOM 3161 C VAL B 193 97.127 26.267 25.310 1.000 23.22 ATOM 3162 O VAL B 193 96.324 26.809 26.074 1.000 16.71 ATOM 3163 N MET B 194 97.131 26.421 23.986 1.000 21.51 ATOM 3164 CA MET B 194 96.216 27.310 23.288 1.000 21.01 ATOM 3165 CB MET B 194 96.933 28.569 22.790 1.000 18.60 ATOM 3166 CG MET B 194 97.200 29.614 23.855 1.000 20.05 ATOM 3167 SD MET B 194 95.704 30.422 24.469 1.000 19.46 ATOM 3168 CE MET B 194 95.163 31.257 22.966 1.000 14.83 ATOM 3169 C MET B 194 95.545 26.611 22.109 1.000 23.67 ATOM 3170 O MET B 194 96.053 25.634 21.564 1.000 19.31 ATOM 3171 N THR B 195 94.381 27.127 21.706 1.000 19.14 ATOM 3172 CA THR B 195 93.691 26.481 20.590 1.000 21.41 ATOM 3173 CB THR B 195 92.552 25.590 21.110 1.000 19.80 ATOM 3174 OG1 THR B 195 93.118 24.424 21.732 1.000 18.08 ATOM 3175 CG2 THR B 195 91.673 25.077 19.981 1.000 20.44 ATOM 3176 C THR B 195 93.172 27.519 19.602 1.000 20.93 ATOM 3177 O THR B 195 92.659 28.565 19.997 1.000 22.89 ATOM 3178 N ILE B 196 93.323 27.219 18.311 1.000 24.23 ATOM 3179 CA ILE B 196 92.772 28.060 17.250 1.000 21.67 ATOM 3180 CB ILE B 196 93.815 28.433 16.185 1.000 18.92 ATOM 3181 CG2 ILE B 196 93.167 29.187 15.035 1.000 11.18 ATOM 3182 CG1 ILE B 196 94.987 29.235 16.746 1.000 18.01 ATOM 3183 CD1 ILE B 196 96.221 29.325 15.871 1.000 23.93 ATOM 3184 C ILE B 196 91.592 27.321 16.617 1.000 19.12 ATOM 3185 O ILE B 196 91.709 26.122 16.356 1.000 19.48 ATOM 3186 N ALA B 197 90.492 28.028 16.405 1.000 17.65 ATOM 3187 CA ALA B 197 89.319 27.474 15.742 1.000 20.33 ATOM 3188 CB ALA B 197 88.076 27.676 16.602 1.000 15.84 ATOM 3189 C ALA B 197 89.119 28.125 14.381 1.000 19.04 ATOM 3190 O ALA B 197 88.425 29.142 14.277 1.000 22.10 ATOM 3191 N PRO B 198 89.708 27.585 13.325 1.000 17.32 ATOM 3192 CD PRO B 198 90.585 26.401 13.272 1.000 15.77 ATOM 3193 CA PRO B 198 89.535 28.199 12.001 1.000 18.83 ATOM 3194 CB PRO B 198 90.466 27.375 11.106 1.000 18.30 ATOM 3195 CG PRO B 198 91.429 26.726 12.052 1.000 17.25 ATOM 3196 C PRO B 198 88.105 28.088 11.492 1.000 17.88 ATOM 3197 O PRO B 198 87.418 27.110 11.741 1.000 22.07 ATOM 3198 N GLY B 199 87.624 29.084 10.753 1.000 17.24 ATOM 3199 CA GLY B 199 86.354 28.939 10.047 1.000 21.59 ATOM 3200 C GLY B 199 86.582 28.289 8.685 1.000 26.45 ATOM 3201 O GLY B 199 86.803 27.077 8.621 1.000 32.80 ATOM 3202 N LEU B 200 86.537 29.074 7.612 1.000 26.29 ATOM 3203 CA LEU B 200 86.750 28.565 6.261 1.000 26.22 ATOM 3204 CB LEU B 200 85.593 28.919 5.337 1.000 30.80 ATOM 3205 CG LEU B 200 84.171 28.547 5.729 1.000 29.38 ATOM 3206 CD1 LEU B 200 83.196 29.355 4.884 1.000 21.97 ATOM 3207 CD2 LEU B 200 83.940 27.051 5.577 1.000 26.34 ATOM 3208 C LEU B 200 88.034 29.129 5.645 1.000 21.47 ATOM 3209 O LEU B 200 88.154 30.343 5.478 1.000 23.70 ATOM 3210 N PHE B 201 88.964 28.244 5.316 1.000 17.48 ATOM 3211 CA PHE B 201 90.280 28.647 4.858 1.000 20.96 ATOM 3212 CB PHE B 201 91.342 28.233 5.887 1.000 20.51 ATOM 3213 CG PHE B 201 91.619 29.319 6.910 1.000 22.85 ATOM 3214 CD1 PHE B 201 90.719 29.547 7.936 1.000 22.28 ATOM 3215 CD2 PHE B 201 92.768 30.090 6.833 1.000 20.32 ATOM 3216 CE1 PHE B 201 90.969 30.543 8.869 1.000 21.15 ATOM 3217 CE2 PHE B 201 93.020 31.086 7.758 1.000 20.28 ATOM 3218 CZ PHE B 201 92.121 31.308 8.785 1.000 20.28 ATOM 3219 C PHE B 201 90.646 28.017 3.521 1.000 25.00 ATOM 3220 O PHE B 201 90.280 26.880 3.226 1.000 24.24 ATOM 3221 N GLY B 202 91.389 28.781 2.726 1.000 28.46 ATOM 3222 CA GLY B 202 91.796 28.281 1.426 1.000 27.60 ATOM 3223 C GLY B 202 92.971 27.335 1.519 1.000 26.65 ATOM 3224 O GLY B 202 94.051 27.658 1.027 1.000 32.79 ATOM 3225 N THR B 203 92.793 26.160 2.102 1.000 24.28 ATOM 3226 CA THR B 203 93.793 25.097 1.999 1.000 26.69 ATOM 3227 CB THR B 203 93.965 24.347 3.324 1.000 27.45 ATOM 3228 OG1 THR B 203 92.784 23.550 3.515 1.000 25.36 ATOM 3229 CG2 THR B 203 94.091 25.273 4.518 1.000 28.01 ATOM 3230 C THR B 203 93.324 24.131 0.918 1.000 28.64 ATOM 3231 O THR B 203 92.175 24.359 0.486 1.000 30.62 ATOM 3232 N PRO B 204 94.072 23.142 0.466 1.000 28.39 ATOM 3233 CD PRO B 204 95.462 22.820 0.828 1.000 28.87 ATOM 3234 CA PRO B 204 93.578 22.220 −0.571 1.000 30.63 ATOM 3235 CB PRO B 204 94.591 21.068 −0.536 1.000 27.82 ATOM 3236 CG PRO B 204 95.859 21.748 −0.140 1.000 27.77 ATOM 3237 C PRO B 204 92.181 21.679 −0.294 1.000 38.86 ATOM 3238 O PRO B 204 91.429 21.401 −1.232 1.000 34.56 ATOM 3239 N LEU B 205 91.836 21.548 0.983 1.000 39.43 ATOM 3240 CA LEU B 205 90.506 21.139 1.411 1.000 33.83 ATOM 3241 CB LEU B 205 90.451 21.293 2.926 1.000 32.03 ATOM 3242 CG LEU B 205 89.410 20.595 3.776 1.000 36.51 ATOM 3243 CD1 LEU B 205 88.999 19.229 3.260 1.000 34.60 ATOM 3244 CD2 LEU B 205 89.964 20.456 5.203 1.000 33.53 ATOM 3245 C LEU B 205 89.426 21.950 0.723 1.000 28.71 ATOM 3246 O LEU B 205 88.378 21.423 0.342 1.000 37.20 ATOM 3247 N LEU B 206 89.636 23.251 0.513 1.000 25.71 ATOM 3248 CA LEU B 206 88.591 24.054 −0.118 1.000 30.76 ATOM 3249 CB LEU B 206 88.240 25.255 0.766 1.000 36.14 ATOM 3250 CG LEU B 206 88.103 24.958 2.263 1.000 40.37 ATOM 3251 CD1 LEU B 206 87.571 26.179 2.997 1.000 60.97 ATOM 3252 CD2 LEU B 206 87.208 23.751 2.492 1.000 33.96 ATOM 3253 C LEU B 206 88.986 24.558 −1.501 1.000 40.20 ATOM 3254 O LEU B 206 88.165 24.616 −2.423 1.000 30.96 ATOM 3255 N THR B 207 90.254 24.941 −1.661 1.000 31.29 ATOM 3256 CA THR B 207 90.678 25.454 −2.963 1.000 39.95 ATOM 3257 CB THR B 207 92.132 25.965 −2.884 1.000 42.48 ATOM 3258 OG1 THR B 207 92.958 24.995 −2.219 1.000 36.55 ATOM 3259 CG2 THR B 207 92.184 27.251 −2.065 1.000 34.71 ATOM 3260 C THR B 207 90.537 24.416 −4.073 1.000 39.41 ATOM 3261 O THR B 207 90.485 24.780 −5.256 1.000 44.36 ATOM 3262 N SER B 208 90.475 23.130 −3.721 1.000 28.72 ATOM 3263 CA SER B 208 90.370 22.082 −4.739 1.000 33.20 ATOM 3264 CB SER B 208 91.057 20.795 −4.288 1.000 33.20 ATOM 3265 OG SER B 208 90.464 20.257 −3.124 1.000 33.13 ATOM 3266 C SER B 208 88.912 21.814 −5.098 1.000 42.89 ATOM 3267 O SER B 208 88.575 20.862 −5.803 1.000 45.91 ATOM 3268 N LEU B 209 88.031 22.681 −4.603 1.000 38.04 ATOM 3269 CA LEU B 209 86.621 22.583 −4.940 1.000 35.13 ATOM 3270 CB LEU B 209 85.756 23.031 −3.768 1.000 39.19 ATOM 3271 CG LEU B 209 85.885 22.257 −2.457 1.000 55.29 ATOM 3272 CD1 LEU B 209 85.627 23.172 −1.267 1.000 60.85 ATOM 3273 CD2 LEU B 209 84.932 21.066 −2.428 1.000 57.75 ATOM 3274 C LEU B 209 86.311 23.435 −6.170 1.000 37.91 ATOM 3275 O LEU B 209 87.022 24.396 −6.475 1.000 30.12 ATOM 3276 N PRO B 210 85.231 23.068 −6.853 1.000 34.73 ATOM 3277 CD PRO B 210 84.373 21.918 −6.548 1.000 34.46 ATOM 3278 CA PRO B 210 84.778 23.819 −8.026 1.000 38.34 ATOM 3279 CB PRO B 210 83.398 23.230 −8.306 1.000 41.74 ATOM 3280 CG PRO B 210 83.425 21.867 −7.706 1.000 41.21 ATOM 3281 C PRO B 210 84.651 25.310 −7.725 1.000 38.15 ATOM 3282 O PRO B 210 84.266 25.712 −6.627 1.000 41.50 ATOM 3283 N GLU B 211 84.980 26.128 −8.717 1.000 32.53 ATOM 3284 CA GLU B 211 84.981 27.576 −8.561 1.000 31.26 ATOM 3285 CB GLU B 211 85.370 28.233 −9.891 1.000 35.90 ATOM 3286 CG GLU B 211 84.870 29.659 −10.046 1.000 43.23 ATOM 3287 CD GLU B 211 85.279 30.303 −11.356 1.000 51.95 ATOM 3288 OE1 GLU B 211 85.853 31.414 −11.323 1.000 62.26 ATOM 3289 OE2 GLU B 211 85.029 29.704 −12.425 1.000 53.28 ATOM 3290 C GLU B 212 83.642 28.099 −8.061 1.000 32.27 ATOM 3291 O GLU B 211 83.581 28.997 −7.213 1.000 21.03 ATOM 3292 N LYS B 212 82.529 27.569 −8.563 1.000 32.31 ATOM 3293 CA LYS B 212 81.243 28.070 −8.071 1.000 38.47 ATOM 3294 CB LYS B 212 80.068 27.458 −8.811 1.000 29.32 ATOM 3295 C LYS B 212 81.148 27.788 −6.577 1.000 43.86 ATOM 3296 O LYS B 212 80.668 28.602 −5.789 1.000 54.98 ATOM 3297 N VAL B 213 81.625 26.598 −6.191 1.000 38.14 ATOM 3298 CA VAL B 213 81.567 26.297 −4.759 1.000 35.85 ATOM 3299 CB VAL B 213 81.926 24.835 −4.467 1.000 38.37 ATOM 3300 CG1 VAL B 213 81.931 24.560 −2.970 1.000 31.23 ATOM 3301 CG2 VAL B 213 80.936 23.914 −5.173 1.000 41.89 ATOM 3302 C VAL B 213 82.476 27.256 −3.998 1.000 31.46 ATOM 3303 O VAL B 213 82.070 27.793 −2.972 1.000 37.88 ATOM 3304 N ARG B 214 83.691 27.495 −4.475 1.000 37.75 ATOM 3305 CA ARG B 214 84.587 28.420 −3.777 1.000 41.19 ATOM 3306 CB ARG B 214 85.934 28.529 −4.503 1.000 39.36 ATOM 3307 CG ARG B 214 86.647 27.190 −4.626 1.000 43.05 ATOM 3308 CD ARG B 214 88.093 27.320 −5.068 1.000 40.23 ATOM 3309 NE ARG B 214 88.247 28.114 −6.277 1.000 35.00 ATOM 3310 CZ ARG B 214 88.345 27.639 −7.512 1.000 39.48 ATOM 3311 NH1 ARG B 214 88.308 26.332 −7.732 1.000 33.49 ATOM 3312 NH2 ARG B 214 88.481 28.477 −8.536 1.000 38.43 ATOM 3313 C ARG B 214 83.922 29.783 −3.624 1.000 33.34 ATOM 3314 O ARG B 214 83.863 30.355 −2.532 1.000 33.42 ATOM 3315 N ASN B 215 83.400 30.309 −4.724 1.000 29.46 ATOM 3316 CA ASN B 215 82.698 31.589 −4.675 1.000 24.27 ATOM 3317 CB ASN B 215 82.091 31.913 −6.036 1.000 27.96 ATOM 3318 CG ASN B 215 83.116 32.178 −7.116 1.000 49.03 ATOM 3319 OD1 ASN B 215 84.318 32.249 −6.853 1.000 61.54 ATOM 3320 ND2 ASN B 215 82.628 32.326 −8.347 1.000 66.34 ATOM 3321 C ASN B 215 81.589 31.563 −3.630 1.000 31.46 ATOM 3322 O ASN B 215 81.385 32.518 −2.888 1.000 40.57 ATOM 3323 N PHE B 216 80.846 30.457 −3.584 1.000 33.81 ATOM 3324 CA PHE B 216 79.719 30.371 −2.665 1.000 34.18 ATOM 3325 CB PHE B 216 78.916 29.090 −2.910 1.000 32.53 ATOM 3326 CG PHE B 216 77.792 28.911 −1.898 1.000 37.68 ATOM 3327 CD1 PHE B 216 76.862 29.916 −1.702 1.000 44.84 ATOM 3328 CD2 PHE B 216 77.680 27.755 −1.153 1.000 45.52 ATOM 3329 CE1 PHE B 216 75.839 29.772 −0.783 1.000 46.68 ATOM 3330 CE2 PHE B 216 76.661 27.599 −0.233 1.000 47.17 ATOM 3331 CZ PHE B 216 75.736 28.610 −0.042 1.000 46.55 ATOM 3332 C PHE B 216 80.187 30.427 −1.211 1.000 39.70 ATOM 3333 O PHE B 216 79.620 31.156 −0.394 1.000 35.84 ATOM 3334 N LEU B 217 81.219 29.643 −0.911 1.000 36.33 ATOM 3335 CA LEU B 217 81.780 29.551 0.430 1.000 30.36 ATOM 3336 CB LEU B 217 82.852 28.461 0.506 1.000 32.88 ATOM 3337 CG LEU B 217 82.298 27.035 0.611 1.000 36.90 ATOM 3338 CD1 LEU B 217 83.363 25.994 0.305 1.000 43.23 ATOM 3339 CD2 LEU B 217 81.693 26.802 1.991 1.000 30.83 ATOM 3340 C LEU B 217 82.332 30.902 0.861 1.000 28.07 ATOM 3341 O LEU B 217 82.036 31.352 1.966 1.000 26.98 ATOM 3342 N ALA B 218 83.107 31.532 −0.015 1.000 27.69 ATOM 3343 CA ALA B 218 83.615 32.869 0.265 1.000 35.60 ATOM 3344 CB ALA B 218 84.459 33.400 −0.887 1.000 31.53 ATOM 3345 C ALA B 218 82.466 33.831 0.527 1.000 35.67 ATOM 3346 O ALA B 218 82.521 34.677 1.416 1.000 30.41 ATOM 3347 N SER B 219 81.411 33.689 −0.277 1.000 35.07 ATOM 3348 CA SER B 219 80.254 34.560 −0.141 1.000 ATOM 3349 CB SER B 219 78.405 33.091 −0.657 1.000 24.81 ATOM 3350 OG SER B 219 78.405 33.091 −0.657 1.000 24.81 ATOM 3351 CB SER B 219 79.634 34.508 1.252 1.000 26.91 ATOM 3352 O SER B 219 78.893 35.438 1.574 1.000 40.31 ATOM 3353 N GLN B 220 79.901 33.478 2.037 1.000 29.34 ATOM 3354 CA GLN B 220 79.337 33.292 3.370 1.000 29.90 ATOM 3355 CB GLN B 220 79.274 31.810 3.738 1.000 36.32 ATOM 3356 CG GLN B 220 78.756 30.911 2.625 1.000 48.32 ATOM 3357 CD GLN B 220 77.429 30.306 3.022 1.000 54.56 ATOM 3358 OE1 GLN B 220 76.375 30.908 2.830 1.000 67.54 ATOM 3359 NE2 GLN B 220 77.491 29.095 3.572 1.000 56.82 ATOM 3360 C GLN B 220 80.138 33.992 4.470 1.000 30.30 ATOM 3361 O GLN B 220 79.662 34.133 5.605 1.000 23.80 ATOM 3362 N VAL B 221 81.375 34.404 4.2.81 1.000 25.59 ATOM 3363 CA VAL B 221 82.170 35.013 5.253 1.000 21.11 ATOM 3364 CB VAL B 221 83.683 34.827 5.056 1.000 18.83 ATOM 3365 CD1 VAL B 221 84.403 35.365 6.287 1.000 14.24 ATOM 3366 CG2 VAL B 221 84.034 33.366 4.799 1.000 14.24 ATOM 3367 C VAL B 221 81.826 36.492 5.318 1.000 24.34 ATOM 3368 O VAL B 221 81.981 37.173 4.296 1.000 26.30 ATOM 3369 N PRO B 222 81.353 37.005 6.445 1.000 23.91 ATOM 3370 CD PRO B 222 81.160 36.335 7.743 1.000 24.90 ATOM 3371 CA PRO B 222 80.914 38.407 6.479 1.000 21.55 ATOM 3372 CB PRO B 222 80.489 38.615 7.940 1.000 19.51 ATOM 3373 CG PRO B 222 80.127 37.233 8.396 1.000 21.27 ATOM 3374 C PRO B 222 81.999 39.392 6.085 1.000 26.91 ATOM 3375 O PRO B 222 81.791 40.209 5.179 1.000 24.96 ATOM 3376 N PHE B 223 83.167 39.377 6.731 1.000 24.34 ATOM 3377 CA PHE B 223 84.216 40.284 6.262 1.000 23.07 ATOM 3378 CB PHE B 223 83.936 41.746 6.649 1.000 21.27 ATOM 3379 CG PHE B 223 85.084 42.637 6.178 1.000 24.70 ATOM 3380 CD1 PHE B 223 85.177 42.994 4.842 1.000 29.09 ATOM 3381 CD2 PHE B 223 86.053 43.094 7.051 1.000 22.56 ATOM 3382 CE1 PHE B 223 86.224 43.781 4.379 1.000 25.41 ATOM 3383 CE2 PHE B 223 87.105 43.869 6.597 1.000 25.23 ATOM 3384 CZ PHE B 223 87.200 44.214 5.258 1.000 21.68 ATOM 3385 C PHE B 223 85.586 39.845 6.784 1.000 27.57 ATOM 3386 O PHE B 223 85.715 39.631 7.997 1.000 23.91 ATOM 3387 N PRO B 224 86.599 39.735 5.933 1.000 28.05 ATOM 3388 CG PRO B 224 87.984 39.411 6.329 1.000 29.64 ATOM 3389 CA PRO B 224 86.504 39.941 4.483 1.000 28.44 ATOM 3390 CB PRO B 224 87.959 40.006 4.022 1.000 30.61 ATOM 3391 CG PRO B 224 88.696 39.180 5.019 1.000 27.95 ATOM 3392 C PRO B 224 85.800 38.774 3.803 1.000 25.89 ATOM 3393 O PRO B 224 85.878 37.651 4.292 1.000 23.18 ATOM 3394 N SER B 225 85.094 39.059 2.716 1.000 26.20 ATOM 3395 CA SER B 225 84.219 38.049 2.125 1.000 28.41 ATOM 3396 CB SER B 225 83.066 38.708 1.367 1.000 37.56 ATOM 3397 OG SER B 225 82.385 39.622 2.211 1.000 54.93 ATOM 3398 CB SER B 225 85.006 37.117 1.215 1.000 28.63 ATOM 3399 O SER B 225 84.844 37.124 −0.003 1.000 28.75 ATOM 3400 N ARG B 226 85.858 36.310 1.832 1.000 22.36 ATOM 3401 CA ARG B 226 86.687 35.359 1.115 1.000 22.82 ATOM 3402 CB ARG B 226 87.892 36.056 0.470 1.000 18.79 ATOM 3403 CG ARG B 226 88.677 36.899 1.473 1.000 21.54 ATOM 3404 CD ARG B 226 90.176 36.733 1.316 1.000 25.20 ATOM 3405 NE ARG B 226 90.922 37.696 2.120 1.000 23.19 ATOM 3406 CZ ARG B 226 91.575 37.367 3.226 1.000 25.07 ATOM 3407 NE1 ARG B 226 92.224 38.304 3.893 1.000 19.90 ATOM 3408 NE2 ARG B 226 91.576 36.114 3.651 1.000 23.08 ATOM 3409 C ARG B 226 87.181 34.273 2.064 1.000 26.25 ATOM 3410 O ARG B 226 87.133 34.410 3.288 1.000 24.82 ATOM 3411 N LEU B 227 87.670 33.187 1.479 1.000 21.51 ATOM 3412 CA LEU B 227 88.281 32.148 2.305 1.000 25.72 ATOM 3413 CE LEU B 227 88.685 30.973 1.412 1.000 25.48 ATOM 3414 CG LEU B 227 87.517 30.370 0.608 1.000 26.39 ATOM 3415 CD1 LEU B 227 88.031 29.371 −0.415 1.000 23.44 ATOM 3416 CD2 LEU B 227 86.495 29.736 1.543 1.000 18.43 ATOM 3417 C LEU B 227 89.453 32.727 3.074 1.000 24.64 ATOM 3418 O LEU B 227 90.092 33.694 2.658 1.000 18.08 ATOM 3419 N GLY B 228 89.760 32.167 4.249 1.000 26.03 ATOM 3420 CA GLY B 228 90.925 32.693 4.964 1.000 22.23 ATOM 3421 C GLY B 228 92.209 32.285 4.257 1.000 20.68 ATOM 3422 O GLY B 228 92.244 31.206 3.651 1.000 22.79 ATOM 3423 N ASP B 229 93.247 33.113 4.332 1.000 20.55 ATOM 3424 CA ASP B 229 94.548 32.733 3.763 1.000 20.20 ATOM 3425 CE ASP B 229 95.305 33.966 3.311 1.000 26.22 ATOM 3426 CG ASP B 229 96.686 33.727 2.742 1.000 37.78 ATOM 3427 OD1 ASP B 229 97.180 34.649 2.055 1.000 50.30 ATOM 3428 OD2 ASP B 229 97.311 32.665 2.942 1.000 36.38 ATOM 3429 C ASP B 229 95.351 31.964 4.809 1.000 18.70 ATOM 3430 O ASP B 229 95.515 32.497 5.906 1.000 22.47 ATOM 3431 N PRO B 230 95.839 30.776 4.487 1.000 24.85 ATOM 3432 CD PRO B 230 95.682 30.076 3.196 1.000 25.08 ATOM 3433 CA PRO B 230 96.623 29.975 5.441 1.000 24.33 ATOM 3434 CE PRO B 230 97.245 28.898 4.543 1.000 26.36 ATOM 3435 CG PRO B 230 96.196 28.690 3.488 1.000 25.22 ATOM 3436 C PRO B 230 97.701 30.776 6.156 1.000 26.10 ATOM 3437 O PRO B 230 98.023 30.510 7.317 1.000 24.78 ATOM 3438 N ALA B 231 98.263 31.777 5.487 1.000 25.30 ATOM 3439 CA ALA B 231 99.260 32.641 6.098 1.000 24.99 ATOM 3440 CB ALA B 231 99.850 33.597 5.081 1.000 21.53 ATOM 3441 C ALA B 231 98.650 33.423 7.260 1.000 27.72 ATOM 3442 O ALA B 231 99.380 33.872 8.142 1.000 23.63 ATOM 3443 N GLU B 232 97.326 33.586 7.249 1.000 23.39 ATOM 3444 CA GLU B 232 96.690 34.297 8.370 1.000 24.37 ATOM 3445 CB GLU B 232 95.313 34.829 7.971 1.000 24.04 ATOM 3446 CG GLU B 232 95.399 35.976 6.963 1.000 22.30 ATOM 3447 CD GLU B 232 94.083 36.265 6.268 1.000 19.98 ATOM 3448 OE1 GLU B 232 93.333 35.320 5.959 1.000 17.23 ATOM 3449 OE2 GLU B 232 93.790 37.451 6.032 1.000 22.71 ATOM 3450 C GLU B 232 96.619 33.387 9.586 1.000 20.32 ATOM 3451 O GLU B 232 96.791 33.821 10.728 1.000 23.31 ATOM 3452 N TYR B 233 96.394 32.097 9.369 1.000 17.51 ATOM 3453 CA TYR B 233 96.485 31.156 10.490 1.000 20.79 ATOM 3454 CB TYR B 233 96.161 29.733 10.043 1.000 18.94 ATOM 3455 CG TYR B 233 96.350 28.654 11.076 1.000 19.81 ATOM 3456 CD1 TYR B 233 95.289 28.296 11.907 1.000 20.70 ATOM 3457 CE1 TYR B 233 95.437 27.303 12.862 1.000 18.77 ATOM 3458 CD2 TYR B 233 97.546 27.974 11.245 1.000 17.63 ATOM 3459 CE2 TYR B 233 97.712 26.992 12.194 1.000 22.14 ATOM 3460 CZ TYR B 233 96.648 26.658 13.007 1.000 22.85 ATOM 3461 OH TYR B 233 96.811 25.672 13.953 1.000 22.40 ATOM 3462 C TYR B 233 97.889 31.236 11.094 1.000 29.44 ATOM 3463 O TYR B 233 98.077 31.335 12.308 1.000 25.44 ATOM 3464 N ALA B 234 98.883 31.168 10.212 1.000 21.62 ATOM 3465 CA ALA B 234 100.282 31.201 10.623 1.000 20.02 ATOM 3466 CE ALA B 234 101.188 31.127 9.400 1.000 24.84 ATOM 3467 C ALA B 234 100.594 32.446 11.440 1.000 17.92 ATOM 3468 O ALA B 234 101.231 32.346 12.492 1.000 25.05 ATOM 3469 N HIS B 235 100.159 33.611 10.977 1.000 17.22 ATOM 3470 CA HIS B 235 100.336 34.841 11.739 1.000 18.97 ATOM 3471 CB HIS B 235 99.660 36.020 11.045 1.000 17.03 ATOM 3472 CG HIS B 235 99.589 37.276 11.854 1.000 21.49 ATOM 3473 CD2 HIS B 235 98.703 37.758 12.765 1.000 22.09 ATOM 3474 ND1 HIS B 235 100.566 38.248 11.751 1.000 26.88 ATOM 3475 CE1 HIS B 235 100.286 39.259 12.561 1.000 24.36 ATOM 3476 NE2 HIS B 235 99.153 38.983 13.195 1.000 25.35 ATOM 3477 C HIS B 235 99.768 34.673 13.150 1.000 24.20 ATOM 3478 O HIS B 235 100.338 35.162 14.127 1.000 20.64 ATOM 3479 N LEU B 236 98.622 33.999 13.272 1.000 24.19 ATOM 3480 CA LEU B 236 98.023 33.863 14.602 1.000 22.43 ATOM 3481 CB LEU B 236 96.560 33.416 14.532 1.000 17.42 ATOM 3482 CG LEU B 236 95.880 33.237 15.902 1.000 16.92 ATOM 3483 CD1 LEU B 236 96.023 34.506 16.729 1.000 16.92 ATOM 3484 CD2 LEU B 236 94.422 32.851 15.744 1.000 16.70 ATOM 3485 C LEU B 236 98.846 32.903 15.456 1.000 21.64 ATOM 3486 O LEU B 236 99.001 33.128 16.659 1.000 20.22 ATOM 3487 N VAL B 237 99.376 31.834 14.868 1.000 19.99 ATOM 3488 CA VAL B 237 100.251 30.929 15.608 1.000 18.28 ATOM 3489 CB VAL B 237 100.792 29.795 14.727 1.000 25.11 ATOM 3490 CG1 VAL B 237 101.981 29.110 15.395 1.000 23.91 ATOM 3491 CG2 VAL B 237 99.705 28.775 14.415 1.000 18.18 ATOM 3492 C VAL B 237 101.415 31.721 16.194 1.000 24.84 ATOM 3493 O VAL B 237 101.774 31.589 17.369 1.000 24.82 ATOM 3494 N GLN B 238 102.015 32.578 15.361 1.000 20.39 ATOM 3495 CA GLN B 238 103.134 33.377 15.837 1.000 21.98 ATOM 3496 CB GLN B 238 103.718 34.217 14.695 1.000 26.47 ATOM 3497 CG GLN B 238 104.840 35.137 15.173 1.000 33.86 ATOM 3498 CD GLN B 238 105.728 35.611 14.040 1.000 45.57 ATOM 3499 OE1 GLN B 238 105.410 35.440 12.861 1.000 45.00 ATOM 3500 NE2 GLN B 238 106.855 36.220 14.396 1.000 42.07 ATOM 3501 C GLN B 238 102.749 34.305 16.984 1.000 22.31 ATOM 3502 O GLN B 238 103.498 34.472 17.950 1.000 26.79 ATOM 3503 N ALA B 239 101.576 34.930 16.875 1.000 18.16 ATOM 3504 CA ALA B 239 101.135 35.872 17.902 1.000 18.40 ATOM 3505 CB ALA B 239 99.819 36.533 17.511 1.000 20.73 ATOM 3506 C ALA B 239 101.018 35.158 19.250 1.000 20.71 ATOM 3507 O ALA B 239 101.457 35.685 20.265 1.000 23.16 ATOM 3508 N ILE B 240 100.450 33.961 19.235 1.000 20.05 ATOM 3509 CA ILE B 240 100.289 33.138 20.426 1.000 25.35 ATOM 3510 CB ILE B 240 99.418 31.904 20.136 1.000 21.83 ATOM 3511 CG2 ILE B 240 99.470 30.903 21.280 1.000 19.47 ATOM 3512 CG1 ILE B 240 97.958 32.221 19.798 1.000 15.52 ATOM 3513 CD1 ILE B 240 97.238 31.016 19.220 1.000 15.32 ATOM 3514 C ILE B 240 101.643 32.700 20.974 1.000 28.29 ATOM 3515 O ILE B 240 101.861 32.715 22.190 1.000 23.76 ATOM 3516 N ILE B 241 102.565 32.318 20.090 1.000 22.50 ATOM 3517 CA ILE B 241 103.911 31.983 20.553 1.000 25.40 ATOM 3518 CB ILE B 241 104.840 31.538 19.407 1.000 27.14 ATOM 3519 CG2 ILE B 241 106.289 31.468 19.869 1.000 20.81 ATOM 3520 CD1 ILE B 241 104.452 30.211 18.738 1.000 21.73 ATOM 3521 CD1 ILE B 241 105.073 30.067 17.356 1.000 19.24 ATOM 3522 C ILE B 241 104.525 33.188 21.253 1.000 23.95 ATOM 3523 O ILE B 241 105.177 33.056 22.288 1.000 22.10 ATOM 3524 N GLU B 242 104.325 34.378 20.686 1.000 19.53 ATOM 3525 CA GLU B 242 105.016 35.554 21.188 1.000 20.82 ATOM 3526 CB GLU B 242 105.098 36.638 20.117 1.000 22.01 ATOM 3527 CG GLU B 242 105.898 36.269 18.878 1.000 25.93 ATOM 3528 CD GLU B 242 105.964 37.432 17.897 1.000 30.65 ATOM 3529 OE1 GLU B 242 106.791 37.382 16.965 1.000 39.62 ATOM 3530 OE2 GLU B 242 105.192 38.405 18.052 1.000 35.25 ATOM 3531 C GLU B 242 104.368 36.145 22.437 1.000 27.37 ATOM 3532 O GLU B 242 105.070 36.770 23.241 1.000 24.53 ATOM 3533 N ASN B 243 103.064 35.975 22.607 1.000 22.12 ATOM 3534 CA ASN B 243 102.369 36.569 23.748 1.000 26.24 ATOM 3535 CB ASN B 243 100.916 36.907 23.391 1.000 21.07 ATOM 3536 CG ASN B 243 100.332 37.907 24.370 1.000 22.04 ATOM 3537 OD1 ASN B 243 100.327 37.675 25.580 1.000 22.80 ATOM 3538 ND2 ASN B 243 99.843 39.030 23.849 1.000 21.75 ATOM 3539 C ASN B 243 102.403 35.645 24.959 1.000 23.87 ATOM 3540 O ASN B 243 101.770 34.588 24.967 1.000 25.67 ATOM 3541 N PRO B 244 103.160 36.009 25.986 1.000 23.78 ATOM 3542 CD PRO B 244 103.897 37.274 26.156 1.000 22.06 ATOM 3543 CA PRO B 244 103.350 35.103 27.127 1.000 23.04 ATOM 3544 CB PRO B 244 104.415 35.814 27.969 1.000 22.47 ATOM 3545 CG PRO B 244 105.017 36.844 27.078 1.000 23.63 ATOM 3546 C PRO B 244 102.099 34.888 27.964 1.000 20.27 ATOM 3547 O PRO B 244 102.063 33.958 28.774 1.000 23.10 ATOM 3548 N PHE B 245 101.068 35.717 27.816 1.000 24.09 ATOM 3549 CA PHE B 245 99.922 35.612 28.728 1.000 19.94 ATOM 3550 CB PHE B 245 99.530 37.003 29.232 1.000 24.39 ATOM 3551 CG PHE B 245 99.015 37.049 30.670 1.000 21.73 ATOM 3552 CD1 PHE B 245 97.758 37.569 30.956 1.000 17.78 ATOM 3553 CD2 PHE B 245 99.799 36.577 31.708 1.000 17.75 ATOM 3554 CE1 PHE B 245 97.290 37.617 32.257 1.000 20.49 ATOM 3555 CE2 PHE B 245 99.324 36.619 33.017 1.000 20.79 ATOM 3556 CZ PHE B 245 98.067 37.132 33.302 1.000 17.74 ATOM 3557 C PHE B 245 98.725 34.925 28.084 1.000 27.35 ATOM 3558 O PHE B 245 97.675 34.806 28.736 1.000 19.89 ATOM 3559 N LEU B 246 98.842 34.471 26.832 1.000 22.36 ATOM 3560 CA LEU B 246 97.762 33.710 26.212 1.000 17.89 ATOM 3561 CB LEU B 246 97.784 33.848 24.686 1.000 22.68 ATOM 3562 CG LEU B 246 97.091 35.100 24.133 1.000 25.09 ATOM 3563 CD1 LEU B 246 97.472 35.302 22.675 1.000 23.65 ATOM 3564 CD2 LEU B 246 95.578 35.009 24.322 1.000 20.52 ATOM 3565 C LEU B 246 97.844 32.238 26.587 1.000 23.42 ATOM 3566 O LEU B 246 98.768 31.511 26.212 1.000 22.20 ATOM 3567 N ASN B 247 96.845 31.782 27.351 1.000 21.98 ATOM 3568 CA ASN B 247 96.882 30.399 27.809 1.000 21.01 ATOM 3569 CB ASN B 247 97.787 30.310 29.039 1.000 21.94 ATOM 3570 CG ASN B 247 98.210 28.908 29.411 1.000 25.84 ATOM 3571 OD1 ASN B 247 98.028 27.941 28.675 1.000 17.45 ATOM 3572 ND2 ASN B 247 98.792 28.782 30.606 1.000 23.37 ATOM 3573 C ASN B 247 95.483 29.883 28.121 1.000 21.43 ATOM 3574 O ASN B 247 94.652 30.609 28.676 1.000 19.82 ATOM 3575 N GLY B 248 95.237 28.628 27.766 1.000 19.48 ATOM 3576 CA GLY B 248 94.013 27.950 28.126 1.000 19.31 ATOM 3577 C GLY B 248 92.796 28.438 27.373 1.000 22.31 ATOM 3578 O GLY B 248 91.663 28.233 27.819 1.000 17.54 ATOM 3579 N GLU B 249 93.031 29.070 26.231 1.000 17.27 ATOM 3580 CA GLU B 249 91.945 29.718 25.494 1.000 16.46 ATOM 3581 CB GLU B 249 92.194 31.218 25.514 1.000 14.25 ATOM 3582 CG GLU B 249 91.391 32.096 24.591 1.000 19.57 ATOM 3583 CG GLU B 249 89.904 32.186 24.864 1.000 21.27 ATOM 3584 OE1 GLU B 249 89.338 33.286 24.699 1.000 24.41 ATOM 3585 OE2 GLU B 249 89.280 31.165 25.211 1.000 21.97 ATOM 3586 C GLU B 249 91.828 29.176 24.072 1.000 24.78 ATOM 3587 O GLU B 249 92.772 28.582 23.534 1.000 19.55 ATOM 3588 N VAL B 250 90.648 29.371 23.494 1.000 21.56 ATOM 3589 CA VAL B 250 90.339 29.004 22.114 1.000 12.85 ATOM 3590 CB VAL B 250 89.143 28.047 22.038 1.000 23.39 ATOM 3591 CG1 VAL B 250 88.826 27.692 20.594 1.000 22.07 ATOM 3592 CG2 VAL B 250 89.418 26.790 22.860 1.000 21.03 ATOM 3593 C VAL B 250 90.048 30.275 21.326 1.000 19.79 ATOM 3594 O VAL B 250 89.234 31.088 21.776 1.000 18.20 ATOM 3595 N ILE B 251 90.692 30.490 20.180 1.000 16.00 ATOM 3596 CA ILE B 251 90.482 31.725 19.431 1.000 17.61 ATOM 3597 CB ILE B 251 91.816 32.468 19.247 1.000 20.13 ATOM 3598 CG2 ILE B 251 91.679 33.615 18.256 1.000 19.21 ATOM 3599 CG1 ILE B 251 92.413 32.951 20.572 1.000 19.68 ATOM 3600 CD1 ILE B 251 93.807 33.526 20.465 1.000 18.52 ATOM 3602 C ILE B 251 89.866 31.466 18.061 1.000 20.08 ATOM 3602 O ILE B 251 90.456 30.740 17.256 1.000 23.04 ATOM 3603 N ARG B 252 88.699 32.046 17.802 1.00021.13 ATOM 3604 CA ARG B 252 88.045 31.910 16.506 1.000 20.87 ATOM 3605 CB ARG B 252 86.572 32.316 16.551 1.000 19.90 ATOM 3606 CG ARG B 252 85.652 31.342 17.277 1.000 22.38 ATOM 3607 CD ARG B 252 84.222 31.909 17.273 1.000 23.90 ATOM 3608 NE ARG B 252 83.591 31.572 15.999 1.000 20.02 ATOM 3609 CZ ARG B 252 82.532 30.796 15.850 1.000 22.56 ATOM 3610 NH1 ARG B 252 82.029 30.538 14.647 1.000 17.65 ATOM 3611 NH2 ARG B 252 81.959 30.267 16.922 1.000 22.29 ATOM 3612 C ARG B 252 88.771 32.770 15.468 1.000 18.40 ATOM 3613 O ARG B 252 88.956 33.959 15.692 1.000 15.46 ATOM 3614 N LEU B 253 89.172 32.173 14.356 1.000 21.76 ATOM 3615 CA LEU B 253 89.827 32.918 13.269 1.000 19.75 ATOM 3616 CB LEU B 253 91.273 32.462 13.119 1.000 16.90 ATOM 3617 CG LEU B 253 92.110 33.141 12.031 1.000 19.36 ATOM 3618 CD1 LEU B 253 92.373 34.599 12.382 1.000 13.74 ATOM 3619 CD2 LEU B 253 93.411 32.381 11.811 1.000 15.37 ATOM 3620 C LEU B 253 89.011 32.685 12.005 1.000 21.76 ATOM 3621 O LEU B 253 89.232 31.685 11.318 1.000 20.48 ATOM 3622 N ASP B 254 88.040 33.556 11.735 1.000 19.57 ATOM 3623 CA ASP B 254 86.997 33.164 10.802 1.000 19.40 ATOM 3624 CB ASP B 254 85.984 32.301 11.591 1.000 13.95 ATOM 3625 CG ASP B 254 85.259 33.087 12.664 1.000 18.25 ATOM 3626 OD1 ASP B 254 85.428 34.315 12.794 1.000 14.45 ATOM 3627 OD2 ASP B 254 84.480 32.462 13.415 1.000 22.32 ATOM 3628 C ASP B 254 86.256 34.300 10.122 1.000 21.71 ATOM 3629 O ASP B 254 85.196 34.050 9.522 1.000 23.65 ATOM 3630 N GLY B 255 86.713 35.539 10.180 1.000 20.84 ATOM 3631 CA GLY B 255 86.027 36.608 9.463 1.000 18.31 ATOM 3632 C GLY B 255 84.584 36.829 9.898 1.000 25.13 ATOM 3633 O GLY B 255 83.783 37.337 9.102 1.000 19.08 ATOM 3634 N ALA B 256 84.280 36.453 11.129 1.000 24.78 ATOM 3635 CA ALA B 256 83.025 36.658 11.830 1.000 21.84 ATOM 3636 CB ALA B 256 82.632 38.133 11.754 1.000 17.70 ATOM 3637 C ALA B 256 81.888 35.778 11.325 1.000 20.87 ATOM 3638 O ALA B 256 80.708 36.023 11.597 1.000 19.77 ATOM 3639 N ILE B 257 82.197 34.716 10.588 1.000 19.51 ATOM 3640 CA ILE B 257 81.157 33.804 10.126 1.000 18.52 ATOM 3641 CB ILE B 257 81.683 32.833 9.057 1.000 16.68 ATOM 3642 CG2 ILE B 257 82.531 31.734 9.681 1.000 23.55 ATOM 3643 CG1 ILE B 257 80.606 32.195 8.177 1.000 18.12 ATOM 3644 CD1 ILE B 257 81.207 31.337 7.073 1.000 15.00 ATOM 3645 C ILE B 257 80.602 32.990 11.291 1.000 24.02 ATOM 3646 O ILE B 257 81.287 32.733 12.283 1.000 19.85 ATOM 3647 N ARG B 258 79.347 32.595 11.153 1.000 21.98 ATOM 3648 CA ARG B 258 78.698 31.606 12.004 1.000 20.95 ATOM 3649 CB ARG B 258 77.670 32.216 12.947 1.000 17.82 ATOM 3650 CG ARG B 258 78.207 33.229 13.949 1.000 17.12 ATOM 3651 CD ARG B 258 79.175 32.588 14.912 1.000 20.59 ATOM 3652 NE ARG B 258 79.702 33.469 15.952 1.000 20.13 ATOM 3653 CZ ARG B 258 80.800 34.200 15.832 1.000 23.28 ATOM 3654 NH1 ARG B 258 81.214 34.974 16.827 1.000 17.97 ATOM 3655 NH2 ARG B 258 81.506 34.173 14.705 1.000 17.45 ATOM 3656 C ARG B 258 78.078 30.576 11.055 1.000 21.87 ATOM 3657 O ARG B 258 77.313 30.946 10.160 1.000 23.38 ATOM 3658 N MET B 259 78.392 29.297 11.206 1.000 21.54 ATOM 3659 CA MET B 259 77.924 28.325 10.220 1.000 22.43 ATOM 3660 CB MET B 259 78.739 27.036 10.336 1.000 23.84 ATOM 3661 CG MET B 259 80.249 27.215 10.293 1.000 28.42 ATOM 3662 SD MET B 259 80.816 28.247 8.932 1.000 29.19 ATOM 3663 CE MET B 259 80.445 27.228 7.511 1.000 26.28 ATOM 3664 C MET B 259 76.447 27.994 10.357 1.000 30.61 ATOM 3665 O MET B 259 75.928 27.762 11.452 1.000 30.15 ATOM 3666 N GLN B 260 75.748 27.953 9.220 1.000 29.07 ATOM 3667 CA GLN B 260 74.339 27.512 9.259 1.000 25.36 ATOM 3668 CB GLN B 260 73.535 28.432 8.343 1.000 31.16 ATOM 3669 CG GLN B 260 72.731 29.454 9.136 1.000 45.72 ATOM 3670 CD GLN B 260 72.532 29.188 10.610 1.000 49.74 ATOM 3671 OE1 GLN B 260 71.445 28.810 11.050 1.000 37.88 ATOM 3672 NE2 GLN B 260 73.538 29.373 11.459 1.000 67.46 ATOM 3673 C GLN B 260 74.247 26.030 8.956 1.000 24.46 ATOM 3674 O GLN B 260 75.291 25.449 8.618 1.000 23.06 ATOM 3675 N PRO B 261 73.101 25.371 9.080 1.000 22.31 ATOM 3676 CD PRO B 261 71.765 25.894 9.433 1.000 28.76 ATOM 3677 CA PRO B 261 73.065 23.921 8.879 1.000 21.73 ATOM 3678 CB PRO B 261 71.567 23.586 8.950 1.000 25.36 ATOM 3679 CG PRO B 261 70.990 24.665 9.805 1.000 27.61 ATOM 3680 C PRO B 261 73.626 23.481 7.530 1.000 26.41 ATOM 3681 OT1 PRO B 261 73.474 24.202 6.525 1.000 28.81 ATOM 3682 OT2 PRO B 261 74.233 22.384 7.508 1.000 28.12 ATOM 3683 PN NAD B 262 94.476 21.958 6.429 1.000 28.31 ATOM 3684 O1N NAD B 262 93.463 22.904 5.865 1.000 34.51 ATOM 3685 O2N NAD B 262 95.865 22.443 6.568 1.000 23.47 ATOM 3686 O3P NAD B 262 94.370 20.567 5.731 1.000 33.68 ATOM 3687 OSM NAD B 262 93.895 21.576 7.886 1.000 30.78 ATOM 3688 C5M NAD B 262 94.768 21.765 9.037 1.000 26.31 ATOM 3689 C4M NAD B 262 93.935 21.757 10.307 1.000 25.70 ATOM 3690 O4M NAD B 262 92.977 22.828 10.156 1.000 29.89 ATOM 3691 C3M NAD B 262 93.132 20.450 10.430 1.000 31.27 ATOM 3692 O3M NAD B 262 92.997 20.071 11.809 1.000 40.08 ATOM 3693 C2M NAD B 262 91.731 20.826 9.885 1.000 32.57 ATOM 3694 O2M NAD B 262 90.747 19.918 10.417 1.000 40.60 ATOM 3695 C1M NAD B 262 91.677 22.240 10.432 1.000 30.08 ATOM 3696 N1N NAD B 262 90.616 23.120 9.899 1.000 37.23 ATOM 3697 C6N NAD B 262 89.624 23.559 10.781 1.000 28.95 ATOM 3698 C5N NAD B 262 88.566 24.365 10.368 1.000 32.41 ATOM 3699 C4N NAD B 262 88.465 24.847 8.942 1.000 33.49 ATOM 3700 C3N NAD B 262 89.608 24.363 8.069 1.000 32.22 ATOM 3701 C2N NAD B 262 90.607 23.542 8.552 1.000 37.43 ATOM 3702 C7N NAD B 262 89.613 24.852 6.631 1.000 36.14 ATOM 3703 O7N NAD B 262 88.579 25.278 6.126 1.000 41.68 ATOM 3704 N7N NAD B 262 90.771 24.795 5.981 1.000 29.37 ATOM 3705 PA NAD B 262 95.272 19.767 4.701 1.000 37.66 ATOM 3706 O1A NAD B 262 94.526 18.562 4.361 1.000 32.50 ATOM 3707 O2A NAD B 262 95.736 20.790 3.767 1.000 30.89 ATOM 3708 O5B NAD B 262 96.478 19.276 5.642 1.000 41.07 ATOM 3709 C5B NAD B 262 96.142 18.219 6.581 1.000 31.86 ATOM 3710 C4B NAD B 262 97.492 17.592 6.832 1.000 27.90 ATOM 3711 O4B NAD B 262 97.270 16.597 7.826 1.000 27.37 ATOM 3712 C3B NAD B 262 97.931 16.870 5.543 1.000 22.88 ATOM 3713 O3B NAD B 262 99.322 17.164 5.210 1.000 29.54 ATOM 3714 C2B NAD B 262 97.702 15.437 5.925 1.000 24.16 ATOM 3715 O2B NAD B 262 98.553 14.519 5.247 1.000 28.28 ATOM 3716 C1B NAD B 262 97.989 15.475 7.430 1.000 26.54 ATOM 3717 N9A NAD B 262 97.552 14.268 8.121 1.000 25.83 ATOM 3718 C4A NAD B 262 98.303 13.579 8.987 1.000 20.78 ATOM 3719 N3A NAD B 262 99.524 13.651 9.529 1.000 17.71 ATOM 3720 C2A NAD B 262 99.938 12.740 10.403 1.000 15.99 ATOM 3721 N1A NAD B 262 99.171 11.723 10.781 1.000 21.15 ATOM 3722 C6A NAD B 262 97.933 11.578 10.284 1.000 27.89 ATOM 3723 C5A NAD B 262 97.508 12.537 9.367 1.000 24.05 ATOM 3724 N7A NAD B 262 96.312 12.565 8.759 1.000 22.87 ATOM 3725 C8A NAD B 262 96.368 13.656 7.986 1.000 18.27 ATOM 3726 N6A NAD B 262 97.174 10.564 10.660 1.000 24.18 ATOM 3727 CB SER C 7 104.044 47.282 9.332 1.000 66.78 ATOM 3728 CB SER C 7 101.832 47.872 10.314 1.000 47.05 ATOM 3729 O SER C 7 100.991 48.304 9.526 1.000 47.44 ATOM 3730 N SER C 7 102.108 45.815 8.998 1.000 59.49 ATOM 3731 CA SER C 7 102.758 46.727 9.929 1.000 50.05 ATOM 3732 N VAL C 8 101.991 48.376 11.537 1.000 41.20 ATOM 3733 CA VAL C 8 101.083 49.420 12.005 1.000 36.25 ATOM 3734 CB VAL C 8 100.808 49.295 13.515 1.000 37.80 ATOM 3735 CG1 VAL C 8 100.118 47.971 13.818 1.000 30.04 ATOM 3736 CG2 VAL C 8 102.100 49.440 14.305 1.000 28.58 ATOM 3737 C VAL C 8 101.644 50.798 11.690 1.000 32.07 ATOM 3738 O VAL C 8 101.009 51.814 11.974 1.000 33.78 ATOM 3739 N LYS C 9 102.836 50.817 11.102 1.000 30.77 ATOM 3740 CA LYS C 9 103.482 52.078 10.746 1.000 29.01 ATOM 3741 CB LYS C 9 104.767 51.812 9.976 1.000 28.15 ATOM 3742 C LYS C 9 102.541 52.963 9.940 1.000 29.94 ATOM 3743 O LYS C 9 101.941 52.514 8.968 1.000 29.66 ATOM 3744 N GLY C 10 102.385 54.215 10.360 1.000 31.59 ATOM 3745 CA GLY C 10 101.522 55.142 9.666 1.000 33.52 ATOM 3746 C GLY C 10 100.057 55.094 10.031 1.000 32.35 ATOM 3747 O GLY C 10 99.310 56.020 9.691 1.000 35.47 ATOM 3748 N LEU C 11 99.599 54.052 10.721 1.000 28.45 ATOM 3749 CA LEU C 11 98.186 53.987 11.099 1.000 25.53 ATOM 3750 CB LEU C 11 97.849 52.594 11.639 1.000 24.47 ATOM 3751 CG LEU C 11 97.907 51.473 10.593 1.000 34.47 ATOM 3752 CD1 LEU C 11 97.628 50.114 11.217 1.000 35.93 ATOM 3753 CD2 LEU C 11 96.927 51.755 9.458 1.000 32.14 ATOM 3754 C LEU C 11 97.824 55.052 12.125 1.000 25.52 ATOM 3755 O LEU C 11 98.680 55.511 12.884 1.000 27.62 ATOM 3756 N VAL C 12 96.557 55.451 12.149 1.000 24.05 ATOM 3757 CA VAL C 12 96.051 56.379 13.153 1.000 24.59 ATOM 3758 CB VAL C 12 95.350 57.592 12.516 1.000 28.40 ATOM 3759 CG1 VAL C 12 94.813 58.519 13.597 1.000 22.74 ATOM 3760 CG2 VAL C 12 96.305 58.326 11.584 1.000 26.07 ATOM 3761 C VAL C 12 95.076 55.672 14.091 1.000 30.65 ATOM 3762 O VAL C 12 94.058 55.119 13.655 1.000 28.77 ATOM 3763 N ALA C 13 95.402 55.687 15.386 1.000 25.84 ATOM 3764 CA ALA C 13 94.551 54.989 16.348 1.000 25.82 ATOM 3765 CB ALA C 13 95.315 53.854 17.018 1.000 25.53 ATOM 3766 C ALA C 13 93.994 55.938 17.407 1.000 26.90 ATOM 3767 O ALA C 13 94.733 56.727 17.992 1.000 28.28 ATOM 3768 N VAL C 14 92.690 55.845 17.641 1.000 23.52 ATOM 3769 CA VAL C 14 92.058 56.564 18.750 1.000 24.13 ATOM 3770 CB VAL C 14 90.708 57.180 18.375 1.000 24.45 ATOM 3771 CG1 VAL C 14 90.033 57.820 19.581 1.000 22.78 ATOM 3772 CG2 VAL C 14 90.876 58.221 17.275 1.000 23.77 ATOM 3773 C VAL C 14 91.912 55.568 19.903 1.000 27.36 ATOM 3774 O VAL C 14 91.304 54.511 19.729 1.000 23.19 ATOM 3775 N ILE C 15 92.497 55.901 21.050 1.000 27.18 ATOM 3776 CA ILE C 15 92.530 55.001 22.199 1.000 20.98 ATOM 3777 CB ILE C 15 93.992 54.654 22.542 1.000 21.64 ATOM 3778 CG2 ILE C 15 94.074 53.721 23.739 1.000 24.49 ATOM 3779 CG1 ILE C 15 94.753 54.070 21.352 1.000 25.53 ATOM 3780 CD1 ILE C 15 96.229 53.822 21.576 1.000 30.45 ATOM 3781 C ILE C 15 91.820 55.612 23.392 1.000 23.68 ATOM 3782 O ILE C 15 92.291 56.563 24.024 1.000 23.20 ATOM 3783 N THR C 16 90.642 55.078 23.734 1.000 23.69 ATOM 3784 CA THR C 16 89.966 55.658 24.904 1.000 24.76 ATOM 3785 CB THR C 16 88.444 55.452 24.868 1.000 22.95 ATOM 3786 OG1 THR C 16 88.140 54.146 25.361 1.000 22.63 ATOM 3787 CG2 THR C 16 87.938 55.536 23.430 1.000 14.61 ATOM 3788 C THR C 16 90.564 55.057 26.172 1.000 17.75 ATOM 3789 O THR C 16 90.998 53.907 26.171 1.000 23.59 ATOM 3790 N GLY C 17 90.594 55.847 27.240 1.000 25.44 ATOM 3791 CA GLY C 17 91.312 55.462 28.451 1.000 21.38 ATOM 3792 C GLY C 17 92.807 55.446 28.172 1.000 26.04 ATOM 3793 O GLY C 17 93.583 54.716 28.787 1.000 26.02 ATOM 3794 N GLY C 18 93.241 56.260 27.212 1.000 25.57 ATOM 3795 CA GLY C 18 94.624 56.224 26.780 1.000 23.27 ATOM 3796 C GLY C 18 95.607 56.901 27.702 1.000 25.52 ATOM 3797 O GLY C 18 96.817 56.861 27.435 1.000 25.03 ATOM 3798 N ALA C 19 95.152 57.541 28.776 1.000 23.60 ATOM 3799 CA ALA C 19 96.093 58.208 29.676 1.000 22.47 ATOM 3800 CB ALA C 19 95.423 59.388 30.373 1.000 21.48 ATOM 3801 C ALA C 19 96.640 57.247 30.715 1.000 28.26 ATOM 3802 O ALA C 19 97.523 57.562 31.516 1.000 25.69 ATOM 3803 N SER C 20 96.107 56.022 30.754 1.000 25.74 ATOM 3804 CA SER C 20 96.517 55.152 31.870 1.000 24.16 ATOM 3805 CB SER C 20 95.640 55.492 33.083 1.000 25.59 ATOM 3806 OG SER C 20 95.760 54.584 34.149 1.000 25.32 ATOM 3807 CB SER C 20 96.449 53.688 31.485 1.000 25.80 ATOM 3808 O SER C 20 95.846 53.324 30.474 1.000 22.31 ATOM 3809 N GLY C 21 97.084 52.851 32.302 1.000 24.52 ATOM 3810 CA GLY C 21 97.035 51.415 32.209 1.000 24.48 ATOM 3811 C GLY C 21 97.032 50.810 30.830 1.000 27.26 ATOM 3812 O GLY C 21 97.934 51.074 30.035 1.000 22.91 ATOM 3813 N LEU C 22 96.052 49.968 30.507 1.000 24.52 ATOM 3814 CA LEU C 22 96.083 49.212 29.254 1.000 21.40 ATOM 3815 CB LEU C 22 94.938 48.195 29.237 1.000 20.78 ATOM 3816 CG LEU C 22 94.886 47.203 30.401 1.000 17.62 ATOM 3817 CD1 LEU C 22 93.684 46.276 30.275 1.000 16.40 ATOM 3818 CD2 LEU C 22 96.149 46.360 30.485 1.000 18.61 ATOM 3819 C LEU C 22 96.032 50.112 28.022 1.000 22.73 ATOM 3820 O LEU C 22 96.725 49.853 27.028 1.000 26.59 ATOM 3821 N GLY C 23 95.224 51.166 28.040 1.000 22.05 ATOM 3822 CA GLY C 23 95.184 52.107 26.934 1.000 26.20 ATOM 3823 C GLY C 23 96.510 52.806 26.694 1.000 25.29 ATOM 3824 O GLY C 23 96.946 52.987 25.552 1.000 23.10 ATOM 3825 N LEU C 24 97.174 53.224 27.756 1.000 19.82 ATOM 3826 CA LEU C 24 98.463 53.904 27.656 1.000 21.17 ATOM 3827 CB LEU C 24 98.914 54.431 29.023 1.000 20.85 ATOM 3828 CG LEU C 24 100.322 55.038 29.077 1.000 25.39 ATOM 3829 CD1 LEU C 24 100.405 56.276 28.194 1.000 21.88 ATOM 3830 CD2 LEU C 24 100.710 55.359 30.513 1.000 24.95 ATOM 3831 C LEU C 24 99.534 52.971 27.109 1.000 23.71 ATOM 3832 O LEU C 24 100.353 53.352 26.274 1.000 26.75 ATOM 3833 N ALA C 25 99.530 51.733 27.596 1.000 23.88 ATOM 3834 CA ALA C 25 100.486 50.731 27.129 1.000 23.51 ATOM 3835 CE ALA C 25 100.339 49.469 27.962 1.000 22.54 ATOM 3836 C ALA C 25 100.294 50.444 25.646 1.000 26.08 ATOM 3837 O ALA C 25 101.252 50.214 24.908 1.000 27.79 ATOM 3838 N THR C 26 99.036 50.458 25.215 1.000 27.03 ATOM 3839 CA THR C 26 98.726 50.283 23.797 1.000 23.27 ATOM 3840 CB THR C 26 97.210 50.151 23.588 1.000 23.63 ATOM 3841 OG1 THR C 26 96.757 49.018 24.341 1.000 24.28 ATOM 3842 CG2 THR C 26 96.879 49.871 22.129 1.000 19.08 ATOM 3843 C THR C 26 99.285 51.445 22.990 1.000 20.18 ATOM 3844 O THR C 26 99.967 51.246 21.983 1.000 26.90 ATOM 3845 N ALA C 27 99.013 52.666 23.438 1.000 18.50 ATOM 3846 CA ALA C 27 99.545 53.852 22.780 1.000 24.38 ATOM 3847 CB ALA C 27 99.097 55.102 23.521 1.000 24.65 ATOM 3848 C ALA C 27 101.065 53.784 22.670 1.000 27.80 ATOM 3849 O ALA C 27 101.645 53.987 21.603 1.000 28.51 ATOM 3850 N GLU C 28 101.754 53.489 23.761 1.000 25.77 ATOM 3851 CA GLU C 28 103.204 53.346 23.738 1.000 28.24 ATOM 3852 CE GLU C 28 103.686 52.865 25.126 1.000 27.28 ATOM 3853 CG GLU C 28 103.837 54.027 26.089 1.000 30.52 ATOM 3854 CG GLU C 28 103.849 53.670 27.559 1.000 36.62 ATOM 3855 OE1 GLU C 28 103.834 54.636 28.356 1.000 39.77 ATOM 3856 OE2 GLU C 28 103.875 52.478 27.938 1.000 39.86 ATOM 3857 C GLU C 28 103.689 52.395 22.657 1.000 29.47 ATOM 3858 O GLU C 28 104.529 52.716 21.819 1.000 24.48 ATOM 3859 N ARG C 29 103.163 51.173 22.643 1.000 26.01 ATOM 3860 CA ARG C 29 103.627 50.179 21.687 1.000 24.39 ATOM 3861 CB ARG C 29 102.929 48.832 21.940 1.000 22.49 ATOM 3862 CG ARG C 29 103.387 47.773 20.954 1.000 25.33 ATOM 3863 CD ARG C 29 102.736 46.417 21.157 1.000 25.09 ATOM 3864 NE ARC C 29 103.371 45.445 20.252 1.000 26.15 ATOM 3865 CZ ARC C 29 104.492 44.805 20.567 1.000 29.99 ATOM 3866 NE1 ARC C 29 105.034 43.943 19.722 1.000 32.98 ATOM 3867 NH2 ARG C 29 105.082 45.024 21.735 1.000 29.67 ATOM 3868 C ARG C 29 103.393 50.615 20.247 1.000 29.05 ATOM 3869 O ARG C 29 104.290 50.524 19.416 1.000 30.10 ATOM 3870 N LEU C 30 102.181 51.074 19.944 1.000 24.61 ATOM 3871 CA LEU C 30 101.845 51.433 18.569 1.000 27.57 ATOM 3872 CE LEU C 30 100.340 51.702 18.463 1.000 27.67 ATOM 3873 CG LEU C 30 99.412 50.514 18.748 1.000 26.24 ATOM 3874 CD1 LEU C 30 97.951 50.907 18.577 1.000 17.98 ATOM 3875 CD2 LEU C 30 99.739 49.330 17.852 1.000 26.64 ATOM 3876 C LEU C 30 102.657 52.632 18.101 1.000 30.46 ATOM 3877 O LEU C 30 103.199 52.663 16.993 1.000 32.23 ATOM 3878 N VAL C 31 102.757 53.649 18.946 1.000 25.35 ATOM 3879 CA VAL C 31 103.564 54.824 18.622 1.000 28.65 ATOM 3880 CE VAL C 31 103.384 55.913 19.688 1.000 34.14 ATOM 3881 CG1 VAL C 31 104.538 56.899 19.707 1.000 41.82 ATOM 3882 CG2 VAL C 31 102.065 56.648 19.435 1.000 29.57 ATOM 3883 C VAL C 31 105.019 54.417 18.474 1.000 30.00 ATOM 3884 O VAL C 31 105.720 54.884 17.575 1.000 34.69 ATOM 3885 N GLY C 32 105.491 53.529 19.341 1.000 25.99 ATOM 3886 CA GLY C 32 106.857 53.035 19.228 1.000 28.69 ATOM 3887 C GLY C 32 107.124 52.338 17.906 1.000 35.56 ATOM 3888 O CLY C 32 108.267 52.191 17.471 1.000 28.87 ATOM 3889 N GLN C 33 106.061 51.887 17.249 1.000 36.98 ATOM 3890 CA GLN C 33 106.139 51.231 15.959 1.000 35.59 ATOM 3891 CB GLN C 33 105.129 50.079 15.896 1.000 39.66 ATOM 3892 CG GLN C 33 105.422 48.955 16.881 1.000 44.72 ATOM 3893 CG GLN C 33 106.200 47.830 16.228 1.000 49.92 ATOM 3894 CE1 GLN C 33 105.897 47.417 15.105 1.000 58.45 ATOM 3895 NE2 GLN C 33 107.213 47.333 16.933 1.000 58.98 ATOM 3896 C GLN C 33 105.857 52.191 14.812 1.000 33.46 ATOM 3897 O GLN C 33 105.688 51.726 13.681 1.000 33.18 ATOM 3898 N GLY C 34 105.779 53.497 15.049 1.000 29.41 ATOM 3899 CA GLY C 34 105.569 54.436 13.961 1.000 29.74 ATOM 3900 C GLY C 34 104.129 54.744 13.625 1.000 34.10 ATOM 3901 O GLY C 34 103.831 55.329 12.575 1.000 29.85 ATOM 3902 N ALA C 35 103.191 54.367 14.501 1.000 31.11 ATOM 3903 CA ALA C 35 101.797 54.764 14.286 1.000 24.85 ATOM 3904 CB ALA C 35 100.850 53.680 14.768 1.000 24.26 ATOM 3905 C ALA C 35 101.518 56.086 14.980 1.000 26.16 ATOM 3906 O ALA C 35 102.344 56.612 15.728 1.000 30.99 ATOM 3907 N SER C 36 100.343 56.674 14.751 1.000 25.80 ATOM 3908 CA SER C 36 100.006 57.889 15.494 1.000 30.50 ATOM 3909 CB SER C 36 99.592 59.028 14.564 1.000 29.64 ATOM 3910 OG SER C 36 100.588 59.261 13.582 1.000 30.71 ATOM 3911 CB SER C 36 98.904 57.581 16.499 1.000 33.79 ATOM 3912 O SER C 36 98.000 56.779 16.254 1.000 29.57 ATOM 3913 N ALA C 37 98.960 58.220 17.667 1.000 30.46 ATOM 3914 CA ALA C 37 97.940 57.900 18.666 1.000 29.38 ATOM 3915 CB ALA C 37 98.571 57.180 19.846 1.000 26.18 ATOM 3916 C ALA C 37 97.195 59.145 19.125 1.000 24.63 ATOM 3917 O ALA C 37 97.739 60.231 19.270 1.000 31.10 ATOM 3918 N VAL C 38 95.903 58.948 19.346 1.000 23.46 ATOM 3919 CA VAL C 38 95.060 59.963 19.960 1.000 25.11 ATOM 3920 CB VAL C 38 93.825 60.332 19.129 1.000 26.80 ATOM 3921 CG1 VAL C 38 92.957 61.323 19.893 1.000 22.47 ATOM 3922 CG2 VAL C 38 94.251 60.893 17.778 1.000 31.11 ATOM 3923 C VAL C 38 94.611 59.420 21.315 1.000 28.98 ATOM 3924 O VAL C 38 93.885 58.425 21.331 1.000 23.94 ATOM 3925 N LEU C 39 95.066 60.051 22.396 1.000 28.48 ATOM 3926 CA LEU C 39 94.646 59.587 23.721 1.000 24.19 ATOM 3927 CB LEU C 39 95.697 59.886 24.775 1.000 24.94 ATOM 3928 CG LEU C 39 97.140 59.481 24.489 1.000 23.07 ATOM 3929 CD1 LEU C 39 98.018 59.768 25.704 1.000 24.37 ATOM 3930 CD2 LEU C 39 97.225 58.014 24.090 1.000 20.30 ATOM 3931 C LEU C 39 93.327 60.247 24.098 1.000 24.84 ATOM 3932 O LEU C 39 93.298 61.411 24.488 1.000 30.15 ATOM 3933 N LEU C 40 92.230 59.509 23.971 1.000 24.08 ATOM 3934 CA LEU C 40 90.934 60.058 24.383 1.000 22.68 ATOM 3935 CB LEU C 40 89.823 59.471 23.529 1.000 18.90 ATOM 3936 CG LEU C 40 88.475 60.190 23.477 1.000 24.88 ATOM 3937 CD1 LEU C 40 87.713 59.786 22.218 1.000 25.54 ATOM 3938 CD2 LEU C 40 87.628 59.900 24.705 1.000 23.21 ATOM 3939 C LEU C 40 90.713 59.765 25.863 1.000 23.80 ATOM 3940 O LEU C 40 90.476 58.618 26.258 1.000 27.07 ATOM 3941 N ASP C 41 90.796 60.777 26.718 1.000 25.76 ATOM 3942 CA ASP C 41 90.600 60.487 28.149 1.000 28.47 ATOM 3943 CB ASP C 41 91.923 60.028 28.746 1.000 21.68 ATOM 3944 CG ASP C 41 91.767 59.043 29.884 1.000 27.64 ATOM 3945 OD1 ASP C 41 90.911 59.267 30.766 1.000 27.48 ATOM 3946 OD2 ASP C 41 92.503 58.037 29.925 1.000 26.03 ATOM 3947 C ASP C 41 90.008 61.697 28.857 1.000 28.20 ATOM 3948 O ASP C 41 89.924 62.770 28.254 1.000 24.75 ATOM 3949 N LEU C 42 89.579 61.540 30.108 1.000 27.88 ATOM 3950 CA LEU C 42 88.935 62.638 30.826 1.000 28.79 ATOM 3951 CB LEU C 42 88.405 62.159 32.179 1.000 27.37 ATOM 3952 CG LEU C 42 87.154 61.285 32.154 1.000 29.50 ATOM 3953 CD1 LEU C 42 86.833 60.741 33.543 1.000 27.78 ATOM 3954 CD2 LEU C 42 85.933 62.040 31.654 1.000 18.12 ATOM 3955 C LEU C 42 89.904 63.797 31.016 1.000 27.41 ATOM 3956 O LEU C 42 91.117 63.609 31.095 1.000 24.79 ATOM 3957 N PRO C 43 89.386 65.018 31.082 1.000 30.98 ATOM 3958 CD PRO C 43 87.971 65.382 30.912 1.000 30.13 ATOM 3959 CA PRO C 43 90.239 66.179 31.336 1.000 29.06 ATOM 3960 CB PRO C 43 89.245 67.330 31.472 1.000 28.41 ATOM 3961 CG PRO C 43 88.035 66.874 30.736 1.000 31.21 ATOM 3962 C PRO C 43 91.032 66.032 32.629 1.000 33.60 ATOM 3963 O PRO C 43 92.161 66.519 32.738 1.000 37.33 ATOM 3964 N ASN C 44 90.481 65.352 33.627 1.000 30.55 ATOM 3965 CA ASN C 44 91.177 65.227 34.903 1.000 40.13 ATOM 3966 CB ASN C 44 90.175 64.806 35.992 1.000 50.07 ATOM 3967 CG ASN C 44 89.303 63.658 35.506 1.000 55.50 ATOM 3968 OD1 ASN C 44 88.190 63.885 35.027 1.000 70.86 ATOM 3969 ND2 ASN C 44 89.810 62.439 35.615 1.000 60.21 ATOM 3970 C ASN C 44 92.324 64.230 34.858 1.000 40.20 ATOM 3971 O ASN C 44 93.177 64.187 35.751 1.000 41.19 ATOM 3972 N SER C 45 92.372 63.388 33.824 1.000 35.46 ATOM 3973 CA SER C 45 93.457 62.399 33.795 1.000 31.90 ATOM 3974 CB SER C 45 93.128 61.324 32.766 1.000 32.38 ATOM 3975 OG SER C 45 93.103 61.854 31.450 1.000 28.70 ATOM 3976 CB SER C 45 94.769 63.103 33.486 1.000 38.08 ATOM 3977 O SER C 45 94.780 64.329 33.327 1.000 65.11 ATOM 3978 N GLY C 46 95.879 62.387 33.388 1.000 35.97 ATOM 3979 CA GLY C 46 97.111 63.008 32.913 1.000 32.68 ATOM 3980 C GLY C 46 97.340 62.706 31.442 1.000 31.30 ATOM 3981 O GLY C 46 98.450 62.427 30.976 1.000 31.52 ATOM 3982 N GLY C 47 96.277 62.742 30.636 1.000 29.98 ATOM 3983 CA GLY C 47 96.481 62.416 29.226 1.000 29.97 ATOM 3984 C GLY C 47 97.432 63.390 28.553 1.000 33.91 ATOM 3985 O GLY C 47 98.246 62.999 27.713 1.000 33.43 ATOM 3986 N GLU C 48 97.323 64.665 28.921 1.000 32.08 ATOM 3987 CA GLU C 48 98.109 65.710 28.283 1.000 31.51 ATOM 3988 CB GLU C 48 97.724 67.092 28.829 1.000 40.11 ATOM 3989 CG GLU C 48 98.026 68.195 27.818 1.000 49.80 ATOM 3990 CD GLU C 48 97.555 67.869 26.411 1.000 59.15 ATOM 3991 OE1 GLU C 48 98.394 67.471 25.570 1.000 67.05 ATOM 3992 OE2 GLU C 48 96.346 68.010 26.125 1.000 70.70 ATOM 3993 C GLU C 48 99.594 65.470 28.468 1.000 30.68 ATOM 3994 O GLU C 48 100.397 65.536 27.540 1.000 35.10 ATOM 3995 N ALA C 49 99.972 65.167 29.703 1.000 32.08 ATOM 3996 CA ALA C 49 101.347 64.793 29.995 1.000 31.11 ATOM 3997 CB ALA C 49 101.531 64.660 31.508 1.000 30.63 ATOM 3998 C ALA C 49 101.746 63.503 29.298 1.000 30.77 ATOM 3999 O ALA C 49 102.884 63.340 28.838 1.000 29.44 ATOM 4000 N GLN C 50 100.846 62.522 29.199 1.000 29.35 ATOM 4001 CA GLN C 50 101.279 61.262 28.586 1.000 26.90 ATOM 4002 CB GLN C 50 100.269 60.141 28.800 1.000 28.09 ATOM 4003 CG GLN C 50 99.978 59.785 30.251 1.000 26.70 ATOM 4004 CG GLN C 50 101.166 59.197 30.982 1.000 32.02 ATOM 4005 OE1 GLN C 50 101.166 59.082 32.210 1.000 48.10 ATOM 4006 NE2 GLN C 50 102.214 58.801 30.271 1.000 22.28 ATOM 4007 C GLN C 50 101.550 61.478 27.096 1.000 27.62 ATOM 4008 O GLN C 50 102.562 61.021 26.560 1.000 30.87 ATOM 4009 N ALA C 51 100.657 62.187 26.428 1.000 27.39 ATOM 4010 CA ALA C 51 100.819 62.514 25.014 1.000 28.62 ATOM 4011 CB ALA C 51 99.605 63.287 24.526 1.000 30.43 ATOM 4012 C ALA C 51 102.098 63.308 24.788 1.000 31.90 ATOM 4013 O ALA C 51 102.817 63.085 23.815 1.000 32.71 ATOM 4014 N LY5 C 52 102.390 64.227 25.704 1.000 31.86 ATOM 4015 CA LY5 C 52 103.638 64.978 25.670 1.000 33.03 ATOM 4016 CB LY5 C 52 103.662 66.008 26.800 1.000 39.70 ATOM 4017 CG LY5 C 52 105.039 66.230 27.402 1.000 53.96 ATOM 4018 CG LY5 C 52 105.132 65.671 28.815 1.000 63.00 ATOM 4019 CE LYS C 52 106.125 64.528 28.890 1.000 69.80 ATOM 4020 NZ LYS C 52 105.816 63.592 30.016 1.000 78.05 ATOM 4021 C LYS C 52 104.831 64.045 25.782 1.000 30.59 ATOM 4022 O LYS C 52 105.826 64.168 25.065 1.000 32.36 ATOM 4023 N LYS C 53 104.769 63.067 26.683 1.000 31.21 ATOM 4024 CA LYS C 53 105.885 62.120 26.736 1.000 35.16 ATOM 4025 CB LYS C 53 105.802 61.244 27.977 1.000 36.21 ATOM 4026 C LYS C 53 105.939 61.247 25.489 1.000 36.60 ATOM 4027 O LYS C 53 107.020 60.790 25.098 1.000 40.19 ATOM 4028 N LEU C 54 104.815 60.969 24.826 1.000 34.36 ATOM 4029 CA LEU C 54 104.927 59.996 23.720 1.000 32.18 ATOM 4030 CB LEU C 54 103.615 59.222 23.560 1.000 27.50 ATOM 4031 CG LEU C 54 103.407 58.081 24.561 1.000 31.07 ATOM 4032 CD1 LEU C 54 102.020 57.479 24.408 1.000 30.58 ATOM 4033 CD2 LEU C 54 104.489 57.021 24.404 1.000 31.81 ATOM 4034 C LEU C 54 105.329 60.632 22.401 1.000 31.63 ATOM 4035 O LEU C 54 105.575 59.930 21.414 1.000 40.05 ATOM 4036 N GLY C 55 105.421 61.960 22.329 1.000 32.10 ATOM 4037 CA GLY C 55 105.961 62.577 21.136 1.000 29.95 ATOM 4038 C GLY C 55 104.947 63.194 20.196 1.000 32.28 ATOM 4039 O GLY C 55 103.735 63.209 20.418 1.000 28.53 ATOM 4040 N ASN C 56 105.486 63.720 19.106 1.000 33.04 ATOM 4041 CA ASN C 56 104.760 64.427 18.070 1.000 38.21 ATOM 4042 CE ASN C 56 105.748 65.028 17.056 1.000 44.18 ATOM 4043 CG ASN C 56 106.691 66.006 17.736 1.000 51.34 ATOM 4044 OD1 ASN C 56 107.868 66.077 17.392 1.000 62.21 ATOM 4045 ND2 ASN C 56 106.166 66.740 18.711 1.000 49.99 ATOM 4046 C ASN C 56 103.766 63.540 17.342 1.000 34.73 ATOM 4047 O ASN C 56 102.839 64.058 16.713 1.000 36.02 ATOM 4048 N ASN C 57 103.925 62.221 17.402 1.000 34.43 ATOM 4049 CA ASN C 57 102.899 61.365 16.805 1.000 33.18 ATOM 4050 CE ASN C 57 103.541 60.105 16.224 1.000 33.00 ATOM 4051 CG ASN C 57 104.198 60.389 14.891 1.000 37.58 ATOM 4052 OD1 ASN C 57 105.119 59.679 14.495 1.000 47.98 ATOM 4053 ND2 ASN C 57 103.734 61.415 14.195 1.000 38.58 ATOM 4054 C ASN C 57 101.813 60.990 17.802 1.000 33.50 ATOM 4055 O ASN C 57 101.035 60.062 17.575 1.000 27.41 ATOM 4056 N CYS C 58 101.751 61.711 18.918 1.000 33.01 ATOM 4057 CA CYS C 58 100.719 61.391 19.908 1.000 31.29 ATOM 4058 CB CYS C 58 101.301 60.555 21.051 1.000 30.99 ATOM 4059 SG CYS C 58 100.105 60.157 22.353 1.000 31.90 ATOM 4060 C CYS C 58 100.076 62.656 20.444 1.000 28.04 ATOM 4061 O CYS C 58 100.747 63.580 20.893 1.000 32.84 ATOM 4062 N VAL C 59 98.745 62.722 20.402 1.000 30.91 ATOM 4063 CA VAL C 59 98.084 63.892 20.974 1.000 29.23 ATOM 4064 CE VAL C 59 97.517 64.839 19.902 1.000 33.71 ATOM 4065 CG1 VAL C 59 98.594 65.184 18.884 1.000 36.94 ATOM 4066 CG2 VAL C 59 96.317 64.225 19.204 1.000 30.60 ATOM 4067 C VAL C 59 96.965 63.455 21.921 1.000 30.45 ATOM 4068 O VAL C 59 96.410 62.366 21.791 1.000 27.62 ATOM 4069 N PHE C 60 96.666 64.341 22.860 1.000 28.52 ATOM 4070 CA PHE C 60 95.618 64.140 23.848 1.000 27.23 ATOM 4071 CE PHE C 60 96.073 64.674 25.208 1.000 27.71 ATOM 4072 CG PHE C 60 94.982 64.718 26.262 1.000 30.69 ATOM 4073 CD1 PHE C 60 94.254 63.580 26.584 1.000 30.34 ATOM 4074 CD2 PHE C 60 94.691 65.899 26.918 1.000 31.41 ATOM 4075 CE1 PHE C 60 93.260 63.630 27.542 1.000 28.34 ATOM 4076 CE2 PHE C 60 93.700 65.958 27.882 1.000 28.62 ATOM 4077 CZ PHE C 60 92.979 64.818 28.190 1.000 26.15 ATOM 4078 C PHE C 60 94.330 64.833 23.424 1.000 31.08 ATOM 4079 O PHE C 60 94.338 66.017 23.092 1.000 30.75 ATOM 4080 N ALA C 61 93.213 64.110 23.432 1.000 28.65 ATOM 4081 CA ALA C 61 91.925 64.751 23.174 1.000 24.00 ATOM 4082 CE ALA C 61 91.280 64.183 21.925 1.000 29.56 ATOM 4083 C ALA C 61 91.026 64.567 24.391 1.000 30.42 ATOM 4084 O ALA C 61 90.471 63.479 24.582 1.000 32.76 ATOM 4085 N PRO C 62 90.882 65.595 25.217 1.000 30.73 ATOM 4086 CD PRO C 62 91.412 66.960 25.062 1.000 28.67 ATOM 4087 CA PRO C 62 90.102 63.446 26.455 1.000 30.54 ATOM 4088 CB PRO C 62 90.213 66.817 27.120 1.000 29.29 ATOM 4089 CG PRO C 62 90.544 67.755 26.004 1.000 30.27 ATOM 4090 C PRO C 62 88.652 65.112 26.132 1.000 30.80 ATOM 4091 O PRO C 62 87.986 65.781 25.338 1.000 31.42 ATOM 4092 N ALA C 63 88.135 64.040 26.739 1.000 26.61 ATOM 4093 CA ALA C 63 86.749 63.698 26.433 1.000 28.05 ATOM 4094 CB ALA C 63 86.632 63.221 24.990 1.000 24.16 ATOM 4095 C ALA C 63 86.204 62.638 27.384 1.000 25.50 ATOM 4096 O ALA C 63 86.947 61.773 27.836 1.000 26.31 ATOM 4097 N ASP C 64 84.904 62.744 27.626 1.000 24.58 ATOM 4098 CA ASP C 64 84.120 61.747 28.329 1.000 27.67 ATOM 4099 CB ASP C 64 83.094 62.409 29.247 1.000 26.67 ATOM 4100 CG ASP C 64 82.271 61.419 30.050 1.000 28.82 ATOM 4101 OD1 ASP C 64 81.576 61.883 30.984 1.000 33.57 ATOM 4102 OD2 ASP C 64 82.294 60.201 29.768 1.000 25.98 ATOM 4103 C ASP C 64 83.426 60.859 27.298 1.000 25.59 ATOM 4104 O ASP C 64 82.706 61.389 26.465 1.000 22.07 ATOM 4105 N VAL C 65 83.639 59.554 27.361 1.000 26.21 ATOM 4106 CA VAL C 65 83.080 58.646 26.369 1.000 24.93 ATOM 4107 CB VAL C 65 83.678 57.227 26.476 1.000 22.24 ATOM 4108 CG1 VAL C 65 85.150 57.2S4 26.085 1.000 16.05 ATOM 4109 CG2 VAL C 65 83.488 56.662 27.874 1.000 22.57 ATOM 4110 C VAL C 65 81.563 58.544 26.450 1.000 23.05 ATOM 4111 O VAL C 65 80.938 58.056 25.506 1.000 25.98 ATOM 4112 N THR C 66 80.938 58.991 27.533 1.000 23.18 ATOM 4113 CA THR C 66 79.481 58.909 27.619 1.000 24.21 ATOM 4114 CB THR C 66 78.997 58.858 29.078 1.000 24.93 ATOM 4115 OG1 THR C 66 79.413 60.068 29.732 1.000 26.10 ATOM 4116 CG2 THR C 66 79.633 57.690 29.823 1.000 25.34 ATOM 4117 C THR C 66 78.803 60.099 26.951 1.000 27.97 ATOM 4118 O THR C 66 77.575 60.186 26.898 1.000 27.71 ATOM 4119 N SER C 67 79.585 61.042 26.442 1.000 26.34 ATOM 4120 CA SER C 67 79.029 62.246 25.852 1.000 25.87 ATOM 4121 CB SER C 67 79.689 63.482 26.475 1.000 21.35 ATOM 4122 OG SER C 67 79.591 64.S78 25.568 1.000 28.25 ATOM 4123 CB SER C 67 79.219 62.277 24.341 1.000 26.46 ATOM 4124 O SER C 67 80.341 62.168 23.844 1.000 29.77 ATOM 4125 N GLU C 68 78.127 62.428 23.610 1.000 28.34 ATOM 4126 CA GLU C 68 78.170 62.504 22.156 1.000 31.50 ATOM 4127 CB GLU C 68 76.753 62.721 21.616 1.000 32.05 ATOM 4128 CG GLU C 68 76.684 62.853 20.104 1.000 33.54 ATOM 4129 CD GLU C 68 75.253 62.873 19.607 1.000 35.59 ATOM 4130 OE1 GLU C 68 74.801 61.833 19.095 1.000 38.18 ATOM 4131 OE2 GLU C 68 74.581 63.915 19.722 1.000 44.21 ATOM 4132 C GLU C 68 79.089 63.626 21.680 1.000 30.11 ATOM 4133 O GLU C 68 79.968 63.428 20.844 1.000 28.18 ATOM 4134 N LYS C 69 78.862 64.808 22.240 1.000 24.11 ATOM 413S CA LYS C 69 79.592 66.004 21.867 1.000 28.20 ATOM 4136 CB LYS C 69 79.047 67.213 22.629 1.000 35.93 ATOM 4137 G LYS C 69 81.089 65.862 22.105 1.000 27.82 ATOM 4138 O LYS C 69 81.906 66.263 21.283 1.000 27.44 ATOM 4139 N ASP C 70 81.475 65.301 23.241 1.000 26.83 ATOM 4140 CA ASP C 70 82.889 65.152 23.559 1.000 27.75 ATOM 4141 CB ASP C 70 83.065 64.567 24.965 1.000 30.47 ATOM 4142 CG ASP C 70 82.823 65.574 26.070 1.000 29.80 ATOM 4143 OD1 ASP C 70 82.332 66.682 25.773 1.000 33.69 ATOM 4144 OD2 ASP C 70 83.117 65.260 27.241 1.000 31.02 ATOM 4145 C ASP C 70 83.586 64.243 22.561 1.000 24.38 ATOM 4146 O ASP C 70 84.688 64.503 22.101 1.000 30.02 ATOM 4147 N VAL C 71 82.952 63.127 22.221 1.000 27.61 ATOM 4148 CA VAL C 71 83.622 62.165 21.339 1.000 26.47 ATOM 4149 CB VAL C 71 82.864 60.834 21.378 1.000 27.37 ATOM 4150 CG1 VAL C 71 83.334 59.880 20.294 1.000 24.28 ATOM 4151 CG2 VAL C 71 83.017 60.198 22.758 1.000 25.10 ATOM 4152 C VAL C 71 83.705 62.753 19.936 1.000 27.36 ATOM 4153 O VAL C 71 84.659 62.525 19.198 1.000 26.11 ATOM 4154 N GLN C 72 82.679 63.523 19.578 1.000 25.77 ATOM 4155 CA GLN C 72 82.674 64.223 18.296 1.000 28.67 ATOM 4156 CB GLN C 72 81.335 64.952 18.120 1.000 28.15 ATOM 4157 CG GLN C 72 80.246 63.991 17.643 1.000 29.52 ATOM 4158 CD GLN C 72 78.888 64.644 17.523 1.000 35.68 ATOM 4159 OE1 GLN C 72 78.543 65.538 18.295 1.000 41.19 ATOM 4160 NE2 GLN C 72 78.111 64.190 16.545 1.000 41.33 ATOM 4161 C GLN C 72 83.847 65.184 18.218 1.000 26.89 ATOM 4162 O GLN C 72 84.553 65.280 17.213 1.000 29.43 ATOM 4163 N THR C 73 84.069 65.908 19.310 1.000 25.94 ATOM 4164 CA THR C 73 85.192 66.835 19.397 1.000 31.15 ATOM 4165 CB THR C 73 85.154 67.610 20.731 1.000 36.88 ATOM 4166 OG1 THR C 73 83.936 68.365 20.792 1.000 35.60 ATOM 4167 CG2 THR C 73 86.302 68.600 20.821 1.000 35.19 ATOM 4168 C THR C 73 86.522 66.114 19.268 1.000 30.75 ATOM 4169 O THR C 73 87.393 66.469 18.471 1.000 34.22 ATOM 4170 N ALA C 74 86.708 65.058 20.060 1.000 23.49 ATOM 4171 CA ALA C 74 87.961 64.318 19.966 1.000 22.59 ATOM 4172 CB ALA C 74 87.997 63.269 21.072 1.000 29.44 ATOM 4173 C ALA C 74 88.145 63.676 18.598 1.000 27.87 ATOM 4174 O ALA C 74 89.250 63.617 18.057 1.000 30.18 ATOM 4175 N LEU C 75 87.069 63.168 17.991 1.000 25.90 ATOM 4176 CA LEU C 75 87.221 62.568 16.671 1.000 27.31 ATOM 4177 CB LEU C 75 85.939 61.827 16.293 1.000 27.10 ATOM 4178 CG LEU C 75 85.631 60.560 17.089 1.000 26.63 ATOM 4179 CD1 LEU C 75 84.376 59.891 16.544 1.000 25.59 ATOM 4180 CD2 LEU C 75 86.809 59.596 17.085 1.000 21.82 ATOM 4181 C LEU C 75 87.570 63.625 15.627 1.000 26.22 ATOM 4182 O LEU C 75 88.385 63.397 14.736 1.000 27.99 ATOM 4183 N ALA C 76 86.965 64.798 15.733 1.000 27.36 ATOM 4184 CA ALA C 76 87.272 65.918 14.852 1.000 32.93 ATOM 4185 CB ALA C 76 86.361 67.096 15.146 1.000 29.31 ATOM 4186 C ALA C 76 88.739 66.314 14.998 1.000 38.15 ATOM 4187 O ALA C 76 89.433 66.565 14.012 1.000 34.89 ATOM 4188 N LEU C 77 89.202 66.352 16.247 1.000 34.23 ATOM 4189 CA LEU C 77 90.606 66.642 16.522 1.000 29.46 ATOM 4190 CB LEU C 77 90.848 66.660 18.026 1.000 31.15 ATOM 4191 CG LEU C 77 92.189 67.144 18.567 1.000 33.61 ATOM 4192 CD1 LEU C 77 92.028 67.757 19.953 1.000 38.66 ATOM 4193 CD2 LEU C 77 93.200 66.013 18.627 1.000 30.53 ATOM 4194 C LEU C 77 91.499 65.619 15.831 1.000 33.47 ATOM 4195 O LEU C 77 92.480 65.970 15.166 1.000 37.01 ATOM 4196 N ALA C 78 91.162 64.338 15.990 1.000 28.96 ATOM 4197 CA ALA C 78 91.990 63.287 15.407 1.000 31.24 ATOM 4198 CB ALA C 78 91.465 61.905 15.761 1.000 32.91 ATOM 4199 C ALA C 78 92.072 63.446 13.891 1.000 31.97 ATOM 4200 O ALA C 78 93.137 63.329 13.293 1.000 33.08 ATOM 4201 N LYS C 79 90.923 63.717 13.284 1.000 33.42 ATOM 4202 CA LYS C 79 90.882 63.915 11.840 1.000 37.37 ATOM 4203 CB LYS C 79 89.446 64.115 11.390 1.000 32.88 ATOM 4204 G LYS C 79 91.777 65.092 11.459 1.000 38.05 ATOM 4205 O LYS C 79 92.616 64.988 10.565 1.000 36.55 ATOM 4206 N GLY C 80 91.582 66.192 12.174 1.000 36.20 ATOM 4207 CA GLY C 80 92.298 67.424 11.934 1.000 40.19 ATOM 4208 C GLY C 80 93.796 67.287 12.069 1.000 42.52 ATOM 4209 O GLY C 80 94.556 67.884 11.303 1.000 42.68 ATOM 4210 N LYS C 81 94.261 66.511 13.043 1.000 36.24 ATOM 4211 CA LYS C 81 95.704 66.397 13.241 1.000 32.94 ATOM 4212 CB LYS C 81 95.971 66.098 14.717 1.000 38.74 ATOM 4213 CG LYS C 81 97.400 65.692 15.034 1.000 46.40 ATOM 4214 CD LYS C 81 98.200 66.940 15.392 1.000 53.53 ATOM 4215 CE LYS C 81 99.576 66.590 15.931 1.000 57.14 ATOM 4216 NZ LYS C 81 100.629 67.536 15.458 1.000 61.84 ATOM 4217 G LYS C 81 96.334 65.319 12.371 1.000 36.28 ATOM 4218 O LYS C 81 97.445 65.464 11.850 1.000 33.53 ATOM 4219 N PHE C 82 95.645 64.189 12.197 1.000 31.94 ATOM 4220 CA PHE C 82 96.300 63.051 11.561 1.000 31.79 ATOM 4221 CB PHE C 82 96.397 61.876 12.544 1.000 35.42 ATOM 4222 CG PHE C 82 97.306 62.153 13.737 1.000 33.42 ATOM 4223 CD1 PHE C 82 98.607 62.586 13.571 1.000 29.90 ATOM 4224 CD2 PHE C 82 96.833 61.979 15.027 1.000 30.22 ATOM 4225 CE1 PHE C 82 99.410 62.839 14.665 1.000 34.59 ATOM 4226 CE2 PHE C 82 97.631 62.218 16.128 1.000 30.43 ATOM 4227 CZ PHE C 82 98.935 62.652 15.953 1.000 32.82 ATOM 4228 C PHE C 82 95.601 62.606 10.284 1.000 31.97 ATOM 4229 O PHE C 82 96.012 61.617 9.681 1.000 33.07 ATOM 4230 N GLY C 83 94.564 63.330 9.882 1.000 36.06 ATOM 4231 CA GLY C 83 93.905 63.142 8.614 1.000 36.63 ATOM 4232 C GLY C 83 92.850 62.066 8.554 1.000 38.62 ATOM 4233 O GLY C 83 91.883 62.213 7.800 1.000 37.81 ATOM 4234 N ARG C 84 93.009 60.993 9.320 1.000 35.39 ATOM 4235 CA ARG C 84 92.071 59.880 9.284 1.000 33.37 ATOM 4236 CB ARG C 84 92.318 58.979 8.067 1.000 28.21 ATOM 4237 CG ARG C 84 93.743 58.498 7.891 1.000 35.27 ATOM 4238 CG ARG C 84 93.826 57.071 7.382 1.000 44.86 ATOM 4239 NE ARG C 84 93.436 56.944 5.991 1.000 51.21 ATOM 4240 CZ ARG C 84 93.063 55.842 5.359 1.000 56.61 ATOM 4241 NE1 ARG C 84 92.734 55.900 4.069 1.000 64.31 ATOM 4242 NE2 ARG C 84 93.001 54.662 5.962 1.000 35.41 ATOM 4243 C ARG C 84 92.154 59.048 10.565 1.000 33.24 ATOM 4244 O ARG C 84 93.077 59.225 11.362 1.000 35.72 ATOM 4245 N VAL C 85 91.184 58.149 10.735 1.000 26.45 ATOM 4246 CA VAL C 85 91.223 57.211 11.857 1.000 26.63 ATOM 4247 CB VAL C 85 90.098 57.408 12.883 1.000 27.68 ATOM 4248 CD1 VAL C 85 90.208 56.362 13.985 1.000 26.03 ATOM 4249 CG2 VAL C 85 90.133 58.808 13.477 1.000 22.07 ATOM 4250 C VAL C 85 91.178 55.785 11.315 1.000 26.47 ATOM 4251 O VAL C 85 90.213 55.387 10.671 1.000 27.69 ATOM 4252 N ASP C 86 92.247 55.035 11.586 1.000 27.28 ATOM 4253 CA ASP C 86 92.348 53.677 11.069 1.000 25.47 ATOM 4254 CB ASP C 86 93.793 53.404 10.635 1.000 25.79 ATOM 4255 CG ASP C 86 94.222 54.369 9.543 1.000 31.04 ATOM 4256 OD1 ASP C 86 95.098 55.218 9.787 1.000 28.57 ATOM 4257 OD2 ASP C 86 93.649 54.261 8.441 1.000 33.34 ATOM 4258 C ASP C 86 91.927 52.636 12.097 1.000 25.22 ATOM 4259 O ASP C 86 91.471 51.552 11.752 1.000 22.72 ATOM 4260 N VAL C 87 92.117 52.981 13.362 1.000 20.25 ATOM 4261 CA VAL C 87 91.938 52.047 14.462 1.000 18.61 ATOM 4262 CB VAL C 87 93.281 51.429 14.889 1.000 25.48 ATOM 4263 CG1 VAL C 87 93.126 50.625 16.171 1.000 24.24 ATOM 4264 CG2 VAL C 87 93.843 50.546 13.778 1.000 23.75 ATOM 4265 C VAL C 87 91.309 52.749 15.661 1.000 23.53 ATOM 4266 O VAL C 87 91.644 53.890 15.975 1.000 24.10 ATOM 4267 N ALA C 88 90.396 52.044 16.322 1.000 22.81 ATOM 4268 CA ALA C 88 89.820 52.530 17.569 1.000 23.04 ATOM 4269 CB ALA C 88 88.371 52.947 17.406 1.000 19.18 ATOM 4270 C ALA C 88 89.957 51.435 18.628 1.000 26.02 ATOM 4271 O ALA C 88 89.630 50.275 18.361 1.000 26.64 ATOM 4272 N VAL C 89 90.447 51.822 19.803 1.000 22.97 ATOM 4273 CA VAL C 89 90.595 50.868 20.901 1.000 22.55 ATOM 4274 CB VAL C 89 92.063 50.633 21.292 1.000 26.76 ATOM 4275 CG1 VAL C 89 92.157 49.550 22.359 1.000 22.89 ATOM 4276 CG2 VAL C 89 92.899 50.249 20.077 1.000 21.77 ATOM 4277 C VAL C 89 89.831 51.369 22.125 1.000 19.84 ATOM 4278 O VAL C 89 90.222 52.384 22.700 1.000 21.07 ATOM 4279 N ASN C 90 88.770 50.668 22.508 1.000 18.37 ATOM 4280 CA ASN C 90 88.013 51.077 23.694 1.000 24.05 ATOM 4281 CB ASN C 90 86.560 50.599 23.584 1.000 21.08 ATOM 4282 CG ASN C 90 85.808 51.301 22.463 1.000 25.47 ATOM 4283 OD1 ASN C 90 85.517 50.707 21.423 1.000 23.05 ATOM 4284 ND2 ASN C 90 85.498 52.578 22.676 1.000 19.99 ATOM 4285 C ASN C 90 88.659 50.558 24.979 1.000 25.39 ATOM 4286 O ASN C 90 88.522 49.381 25.323 1.000 22.97 ATOM 4287 N CYS C 91 89.374 51.440 25.685 1.000 20.95 ATOM 4288 CA CYS C 91 89.929 51.040 26.976 1.000 24.57 ATOM 4289 CB CYS C 91 91.455 51.216 26.981 1.000 24.07 ATOM 4290 SG CYS C 91 92.321 49.981 25.961 1.000 24.05 ATOM 4291 C CYS C 91 89.304 51.806 28.136 1.000 24.51 ATOM 4292 O CYS C 91 89.453 51.395 29.290 1.000 23.54 ATOM 4293 N ALA C 92 88.606 52.908 27.884 1.000 23.37 ATOM 4294 CA ALA C 92 87.988 53.646 28.991 1.000 27.55 ATOM 4295 CB ALA C 92 87.234 54.856 28.466 1.000 16.49 ATOM 4296 C ALA C 92 87.063 52.747 29.808 1.000 30.67 ATOM 4297 O ALA C 92 86.174 52.068 29.271 1.000 22.30 ATOM 4298 N GLY C 93 87.263 52.718 31.131 1.000 24.95 ATOM 4299 CA GLY C 93 86.399 51.890 31.957 1.000 21.65 ATOM 4300 C GLY C 93 86.592 52.105 33.444 1.000 26.09 ATOM 4301 O GLY C 93 87.604 52.633 33.902 1.000 21.98 ATOM 4302 N ILE C 94 85.600 51.700 34.228 1.000 24.72 ATOM 4303 CA ILE C 94 85.639 51.835 35.682 1.000 20.97 ATOM 4304 CB ILE C 94 84.789 53.009 36.177 1.000 21.91 ATOM 4305 CG2 ILE C 94 85.395 54.339 35.748 1.000 25.24 ATOM 4306 CD1 ILE C 94 83.326 52.933 35.735 1.000 26.80 ATOM 4307 CD1 THR C 94 82.402 53.851 36.510 1.000 28.94 ATOM 4308 C ILE C 94 85.121 50.552 36.321 1.000 25.27 ATOM 4309 O ILE C 94 84.464 49.767 35.639 1.000 20.88 ATOM 4310 N ALA C 95 85.413 50.354 37.596 1.000 31.52 ATOM 4311 CA ALA C 95 85.032 49.161 38.336 1.000 31.13 ATOM 4312 CB ALA C 95 86.266 48.327 38.644 1.000 24.85 ATOM 4313 C ALA C 95 84.336 49.510 39.642 1.000 29.69 ATOM 4314 O ALA C 95 84.583 50.576 40.208 1.000 26.96 ATOM 4315 N VAL C 96 83.483 48.626 40.137 1.000 26.02 ATOM 4316 CA VAL C 96 82.972 48.747 41.493 1.000 24.18 ATOM 4317 CB VAL C 96 81.621 49.475 41.630 1.000 34.59 ATOM 4318 CG1 VAL C 96 81.680 50.876 41.043 1.000 51.91 ATOM 4319 CG2 VAL C 96 80.504 48.674 40.977 1.000 37.98 ATOM 4320 C VAL C 96 82.807 47.349 42.081 1.000 23.92 ATOM 4321 O VAL C 96 82.559 46.370 41.386 1.000 25.46 ATOM 4322 N ALA C 97 82.941 47.232 43.398 1.000 22.45 ATOM 4323 CA ALA C 97 82.609 45.956 44.034 1.000 18.77 ATOM 4324 CB ALA C 97 83.802 45.389 44.753 1.000 28.21 ATOM 4325 C ALA C 97 81.424 46.210 44.957 1.000 25.22 ATOM 4326 O ALA C 97 81.513 47.063 45.845 1.000 29.86 ATOM 4327 N SER C 98 80.327 45.506 44.731 1.000 23.38 ATOM 4328 CA SER C 98 79.141 45.722 45.577 1.000 25.77 ATOM 4329 CB SER C 98 78.519 47.070 45.248 1.000 24.89 ATOM 4330 OG SER C 98 77.352 47.382 45.971 1.000 22.27 ATOM 4331 CB SER C 98 78.192 44.551 45.385 1.000 25.87 ATOM 4332 O SER C 98 77.767 44.267 44.262 1.000 21.71 ATOM 4333 N LYS C 99 77.878 43.851 46.468 1.000 19.96 ATOM 4334 CA LYS C 99 76.949 42.736 46.442 1.000 24.20 ATOM 4335 CE LYS C 99 76.821 42.103 47.829 1.000 25.97 ATOM 4336 CG LYS C 99 78.029 41.351 48.356 1.000 28.65 ATOM 4337 CD LYS C 99 77.583 40.149 49.176 1.000 31.25 ATOM 4338 CE LYS C 99 78.568 39.776 50.268 1.000 38.05 ATOM 4339 NZ LYS C 99 77.913 38.887 51.278 1.000 51.74 ATOM 4340 C LYS C 99 75.544 43.156 46.018 1.000 25.56 ATOM 4341 O LYS C 99 75.089 44.241 46.380 1.000 25.47 ATOM 4342 N THR C 100 74.855 42.300 45.278 1.000 21.51 ATOM 4343 CA THR C 100 73.478 42.560 44.866 1.000 17.21 ATOM 4344 CB THR C 100 72.898 41.354 44.112 1.000 22.90 ATOM 4345 OG1 THR C 100 73.639 41.178 42.892 1.000 24.84 ATOM 4346 CG2 THR C 100 71.440 41.604 43.740 1.000 23.05 ATOM 4347 C THR C 100 72.596 42.860 46.076 1.000 23.89 ATOM 4348 O THR C 100 71.833 43.819 46.092 1.000 22.63 ATOM 4349 N TYR C 101 72.737 42.017 47.093 1.000 23.56 ATOM 4350 CA TYR C 101 72.063 42.148 48.366 1.000 23.20 ATOM 4351 CB TYR C 101 70.660 41.516 48.343 1.000 20.29 ATOM 4352 CG TYR C 101 69.964 41.701 49.688 1.000 25.09 ATOM 4353 CD1 TYR C 101 69.746 40.620 50.525 1.000 25.63 ATOM 4354 CE1 TYR C 101 69.122 40.784 51.744 1.000 29.97 ATOM 4355 CD2 TYR C 101 69.550 42.958 50.107 1.000 27.65 ATOM 4356 CE2 TYR C 101 68.920 43.133 51.330 1.000 31.37 ATOM 4357 CZ TYR C 101 68.711 42.037 52.143 1.000 32.86 ATOM 4358 OH TYR C 101 68.089 42.179 53.362 1.000 34.12 ATOM 4359 C TYR C 101 72.892 41.502 49.476 1.000 27.30 ATOM 4360 O TYR C 101 73.412 40.404 49.274 1.000 25.60 ATOM 4361 N ASN C 102 73.006 42.164 50.622 1.000 29.43 ATOM 4362 CA ASN C 102 73.716 41.595 51.770 1.000 28.87 ATOM 4363 CB ASN C 102 74.869 42.506 52.184 1.000 30.71 ATOM 4364 CG ASN C 102 75.751 41.924 53.273 1.000 34.19 ATOM 4365 OD1 ASN C 102 75.292 41.152 54.113 1.000 33.00 ATOM 4366 ND2 ASN C 102 77.031 42.283 53.289 1.000 23.49 ATOM 4367 C ASN C 102 72.762 41.379 52.941 1.000 24.06 ATOM 4368 O ASN C 102 72.368 42.358 53.583 1.000 28.89 ATOM 4369 N LEU C 103 72.388 40.138 53.225 1.000 24.08 ATOM 4370 CA LEU C 103 71.398 39.899 54.278 1.000 30.00 ATOM 4371 CB LEU C 103 70.947 38.441 54.299 1.000 28.45 ATOM 4372 CG LEU C 103 69.917 38.042 55.361 1.000 32.39 ATOM 4373 CD1 LEU C 103 68.610 38.804 55.196 1.000 33.98 ATOM 4374 CD2 LEU C 103 69.651 36.543 55.326 1.000 25.45 ATOM 4375 C LEU C 103 71.933 40.322 55.646 1.000 35.26 ATOM 4376 O LEU C 103 71.299 41.113 56.348 1.000 38.65 ATOM 4377 N LYS C 104 73.090 39.802 56.024 1.000 39.01 ATOM 4378 CA LYS C 104 73.708 40.104 57.306 1.000 41.66 ATOM 4379 CB LYS C 104 75.103 39.498 57.386 1.000 47.98 ATOM 4380 C LYS C 104 73.770 41.607 57.562 1.000 38.16 ATOM 4381 O LYS C 104 73.509 42.058 58.678 1.000 44.94 ATOM 4382 N LYS C 105 74.103 42.377 56.534 1.000 32.61 ATOM 4383 CA LYS C 105 74.220 43.824 56.663 1.000 33.58 ATOM 4384 CB LYS C 105 7S.308 44.376 55.741 1.000 40.90 ATOM 4385 CG LYS C 105 76.696 44.469 56.339 1.00O 51.19 ATOM 4386 CD LYS C 105 77.585 45.413 55.548 1.000 62.16 ATOM 4387 CE LYS C 105 76.859 46.019 54.356 1.000 69.04 ATOM 4388 NZ LYS C 105 77.114 47.481 54.221 1.000 70.89 ATOM 4389 C LYS C 105 72.908 44.517 56.323 1.000 30.56 ATOM 4390 O LYS C 105 72.767 45.726 56.514 1.000 30.90 ATOM 4391 N GLY C 106 71.950 43.761 55.790 1.000 26.43 ATOM 4392 CA GLY C 106 70.712 44.375 55.311 1.000 27.03 ATOM 4393 C GLY C 106 71.008 45.502 54.337 1.000 27.69 ATOM 4394 O GLY C 106 70.444 46.595 54.418 1.000 32.58 ATOM 4395 N GLN C 107 71.925 45.261 53.399 1.000 29.25 ATOM 4396 CA GLN C 107 72.291 46.325 52.464 1.000 29.86 ATOM 4397 CB GLN C 107 73.738 46.748 52.653 1.000 28.35 ATOM 4398 C GLN C 107 72.049 45.893 51.016 1.000 29.83 ATOM 4399 O GLN C 107 72.332 44.747 50.660 1.000 25.04 ATOM 4400 N THR C 108 71.525 46.830 50.239 1.000 27.41 ATOM 4401 CA THR C 108 71.163 46.631 48.847 1.000 28.51 ATOM 4402 CB THR C 108 69.712 47.082 48.588 1.000 26.57 ATOM 4403 OD1 THR C 108 68.811 46.331 49.402 1.000 23.48 ATOM 4404 CG2 THR C 108 69.313 46.770 47.151 1.000 26.36 ATOM 4405 C THR C 108 72.078 47.398 47.899 1.000 22.28 ATOM 4406 O THR C 108 72.327 48.582 48.122 1.000 21.53 ATOM 4407 N HIS C 109 72.564 46.729 46.859 1.000 25.01 ATOM 4408 CA HIS C 109 73.295 47.402 45.783 1.000 22.12 ATOM 4409 CB HIS C 109 73.530 46.456 44.612 1.000 23.18 ATOM 4410 CG HIS C 109 74.490 46.905 43.558 1.000 21.71 ATOM 4411 CD2 HIS C 109 75.506 46.241 42.955 1.000 22.92 ATOM 4412 ND1 HIS C 109 74.482 48.155 42.986 1.000 20.66 ATOM 4413 CE1 HIS C 109 75.447 48.248 42.084 1.000 21.46 ATOM 4414 NE2 HIS C 109 76.089 47.098 42.044 1.000 21.40 ATOM 4415 C HIS C 109 72.508 48.624 45.334 1.000 20.47 ATOM 4416 O HIS C 109 71.301 48.553 45.084 1.000 25.75 ATOM 4417 N THR C 110 73.153 49.786 45.235 1.000 20.46 ATOM 4418 CA THR C 110 72.348 50.934 44.829 1.000 21.09 ATOM 4419 CB THR C 110 72.993 52.284 45.189 1.000 22.39 ATOM 4420 OG1 THR C 110 74.177 52.416 44.393 1.000 24.12 ATOM 4421 CG2 THR C 110 73.375 52.322 46.661 1.000 20.02 ATOM 4422 C THR C 110 72.118 50.930 43.325 1.000 24.72 ATOM 4423 O THR C 110 72.919 50.413 42.558 1.000 29.03 ATOM 4424 N LEU C 111 71.002 51.524 42.921 1.000 25.48 ATOM 4425 CA LEU C 111 70.718 51.623 41.495 1.000 24.76 ATOM 4426 CB LEU C 111 69.317 52.216 41.309 1.000 25.46 ATOM 4427 CG LEU C 111 68.749 52.087 39.890 1.000 25.35 ATOM 4428 CD1 LEU C 111 68.710 50.626 39.469 1.000 22.50 ATOM 4429 CD2 LEU C 111 67.374 52.735 39.816 1.000 27.56 ATOM 4430 C LEU C 111 71.772 52.457 40.786 1.000 25.44 ATOM 4431 O LEU C 111 72.270 52.101 39.719 1.000 23.31 ATOM 4432 N GLU C 112 72.163 53.605 41.348 1.000 25.18 ATOM 4433 CA GLU C 112 73.093 54.443 40.590 1.000 31.68 ATOM 4434 CB GLU C 112 73.186 55.837 41.215 1.000 41.48 ATOM 4435 CG GLU C 112 72.266 56.860 40.577 1.000 58.29 ATOM 4436 CD GLU C 112 71.704 56.498 39.220 1.000 62.69 ATOM 4437 OE1 GLU C 112 72.217 57.028 38.204 1.000 56.30 ATOM 4438 OE2 GLU C 112 70.738 55.700 39.142 1.000 39.60 ATOM 4439 C GLU C 112 74.479 53.821 40.454 1.000 29.28 ATOM 4440 O GLU C 112 75.175 54.140 39.479 1.000 21.19 ATOM 4441 N ASP C 113 74.898 52.960 41.375 1.000 26.57 ATOM 4442 CA ASP C 113 76.177 52.263 41.200 1.000 24.79 ATOM 4443 CB ASP C 113 76.544 51.445 42.428 1.000 24.71 ATOM 4444 CG ASP C 113 77.406 52.158 43.439 1.000 26.72 ATOM 4445 OD1 ASP C 113 78.053 53.164 43.098 1.000 25.92 ATOM 4446 OD2 ASP C 113 77.449 51.724 44.608 1.000 30.58 ATOM 4447 C ASP C 113 76.101 51.338 39.986 1.000 21.47 ATOM 4448 O ASP C 113 77.048 51.172 39.224 1.000 26.34 ATOM 4449 N PHE C 114 74.942 50.711 39.794 1.000 19.80 ATOM 4450 CA PHE C 114 74.759 49.855 38.624 1.000 21.89 ATOM 4451 CB PHE C 114 73.493 49.015 38.774 1.000 21.43 ATOM 4452 CG PHE C 114 73.344 47.960 37.684 1.000 22.40 ATOM 4453 CD1 PHE C 114 72.610 48.247 36.541 1.000 22.43 ATOM 4454 CD2 PHE C 114 73.933 46.719 37.817 1.000 18.60 ATOM 4455 CE1 PHE C 114 72.485 47.298 35.551 1.000 21.11 ATOM 4456 CE2 PHE C 114 73.803 45.764 36.826 1.000 23.20 ATOM 4457 CZ PHE C 114 73.068 46.053 35.693 1.000 16.97 ATOM 4458 C PHE C 114 74.702 50.692 37.346 1.000 22.83 ATOM 4459 O PHE C 114 75.297 50.331 36.333 1.000 25.15 ATOM 4460 N GLN C 115 73.991 51.808 37.403 1.000 21.70 ATOM 4461 CA GLN C 115 73.818 52.709 36.281 1.000 26.11 ATOM 4462 CB GLN C 115 72.795 53.799 36.630 1.000 26.45 ATOM 4463 CG GLN C 115 72.395 54.654 35.434 1.000 30.61 ATOM 4464 CD GLN C 115 71.550 53.875 34.441 1.000 33.27 ATOM 4465 OE1 GLN C 115 70.493 53.348 34.790 1.000 33.80 ATOM 4466 NE2 GLN C 115 72.024 53.798 33.202 1.000 30.59 ATOM 4467 C GLN C 115 75.117 53.375 35.839 1.000 26.35 ATOM 4468 O GLN C 115 75.372 53.460 34.632 1.000 28.81 ATOM 4469 N ARG C 116 75.923 53.849 36.784 1.000 19.66 ATOM 4470 CA ARG C 116 77.158 54.545 36.427 1.000 21.15 ATOM 4471 CB ARG C 116 77.751 55.189 37.675 1.000 26.20 ATOM 4472 C ARG C 116 78.179 53.619 35.783 1.000 22.02 ATOM 4473 O ARG C 116 78.970 53.981 34.907 1.000 24.22 ATOM 4474 N VAL C 117 78.204 52.359 36.213 1.000 21.35 ATOM 4475 CA VAL C 117 79.119 51.397 35.597 1.000 20.76 ATOM 4476 CB VAL C 117 79.266 50.152 36.481 1.000 21.27 ATOM 4477 CG1 VAL C 117 79.904 49.002 35.725 1.000 19.89 ATOM 4478 CG2 VAL C 117 80.101 50.504 37.711 1.000 26.91 ATOM 4479 C VAL C 117 78.649 51.028 34.196 1.000 21.72 ATOM 4480 O VAL C 117 79.461 50.885 33.281 1.000 27.53 ATOM 4481 N LEU C 118 77.347 50.875 34.001 1.000 21.28 ATOM 4482 CA LEU C 118 76.767 50.593 32.699 1.000 22.07 ATOM 4483 CB LEU C 118 75.257 50.445 32.813 1.000 22.40 ATOM 4484 CG LEU C 118 74.619 49.086 33.041 1.000 34.91 ATOM 4485 CD1 LEU C 118 73.187 49.096 32.499 1.000 33.59 ATOM 4486 CD2 LEU C 118 75.415 47.952 32.414 1.000 37.45 ATOM 4487 C LEU C 118 77.062 51.715 31.693 1.000 25.15 ATOM 4488 O LEU C 118 77.454 51.474 30.554 1.000 22.17 ATOM 4489 N ASP C 119 76.840 52.945 32.142 1.000 25.17 ATOM 4490 CA ASP C 119 77.042 54.136 31.331 1.000 23.07 ATOM 4491 CB ASP C 119 76.673 55.397 32.119 1.000 21.46 ATOM 4492 CG ASP C 119 75.171 55.573 32.250 1.000 24.19 ATOM 4493 OD1 ASP C 119 74.732 56.626 32.757 1.000 35.16 ATOM 4494 OD2 ASP C 119 74.428 54.649 31.852 1.000 26.39 ATOM 4495 C ASP C 119 78.473 54.263 30.817 1.000 30.13 ATOM 4496 O ASP C 119 78.692 54.440 29.608 1.000 22.50 ATOM 4497 N VAL C 120 79.466 54.183 31.709 1.000 24.43 ATOM 4498 CA VAL C 120 80.837 54.384 31.223 1.000 22.41 ATOM 4499 CB VAL C 120 81.829 54.644 32.372 1.000 23.24 ATOM 4500 CG1 VAL C 120 83.263 54.680 31.870 1.000 22.29 ATOM 4501 CG2 VAL C 120 81.508 55.957 33.077 1.000 24.06 ATOM 4502 C VAL C 120 81.316 53.194 30.406 1.000 17.91 ATOM 4503 O VAL C 120 81.848 53.385 29.305 1.000 26.22 ATOM 4504 N ASN C 121 81.146 51.974 30.908 1.000 13.92 ATOM 4505 CA ASN C 121 81.797 50.821 30.295 1.000 18.63 ATOM 4506 CB ASN C 121 81.877 49.626 31.250 1.000 20.72 ATOM 4507 CG ASN C 121 82.729 49.879 32.474 1.000 24.64 ATOM 4508 OD1 ASN C 121 83.339 50.939 32.605 1.000 23.75 ATOM 4509 ND2 ASN C 121 82.776 48.902 33.373 1.000 21.68 ATOM 4510 C ASN C 121 81.108 50.345 29.023 1.000 19.66 ATOM 4511 O ASN C 121 81.782 49.961 28.060 1.000 22.39 ATOM 4512 N LEU C 122 79.784 50.343 29.034 1.000 21.72 ATOM 4513 CA LEU C 122 79.019 49.750 27.940 1.000 18.43 ATOM 4514 CE LEU C 122 77.882 48.904 28.508 1.000 17.19 ATOM 4515 CG LEU C 122 76.918 48.259 27.511 1.000 21.34 ATOM 4516 CD1 LEU C 122 77.683 47.507 26.435 1.000 18.33 ATOM 4517 CD2 LEU C 122 75.938 47.348 28.237 1.000 16.15 ATOM 4518 C LEU C 122 78.500 50.817 26.990 1.000 21.38 ATOM 4519 O LEU C 122 78.807 50.810 25.796 1.000 28.84 ATOM 4520 N MET C 123 77.706 51.739 27.510 1.000 19.47 ATOM 4521 CA MET C 123 77.180 52.834 26.709 1.000 21.09 ATOM 4522 CE MET C 123 76.191 53.662 27.528 1.000 23.37 ATOM 4523 CG MET C 123 75.557 54.811 26.761 1.000 25.26 ATOM 4524 SD MET C 123 76.474 56.352 26.889 1.000 27.76 ATOM 4525 CE MET C 123 76.109 56.826 28.585 1.000 24.30 ATOM 4526 C MET C 123 78.311 53.710 26.186 1.000 26.12 ATOM 4527 O MET C 123 78.294 54.131 25.026 1.000 27.11 ATOM 4528 N GLY C 124 79.294 53.998 27.025 1.000 23.16 ATOM 4529 CA GLY C 124 80.457 54.773 26.620 1.000 24.75 ATOM 4530 C GLY C 124 81.211 54.112 25.479 1.000 26.45 ATOM 4531 O GLY C 124 81.589 54.753 24.500 1.000 23.18 ATOM 4532 N THR C 125 81.440 52.807 25.577 1.000 22.27 ATOM 4533 CA THR C 125 82.099 52.096 24.480 1.000 20.93 ATOM 4534 CE THR C 125 82.436 50.653 24.889 1.000 21.42 ATOM 4535 OG1 THR C 125 83.661 50.663 25.648 1.000 21.32 ATOM 4536 CG2 THR C 125 82.677 49.761 23.677 1.000 21.31 ATOM 4537 C THR C 125 81.232 52.132 23.227 1.000 22.04 ATOM 4538 O THR C 125 81.731 52.449 22.141 1.000 22.04 ATOM 4539 N PHE C 126 79.938 51.849 23.321 1.000 22.32 ATOM 4540 CA PHE C 126 79.086 51.916 22.134 1.000 23.46 ATOM 4541 CB PHE C 126 77.644 51.478 22.431 1.000 17.51 ATOM 4542 CG PHE C 126 76.778 51.434 21.177 1.000 26.11 ATOM 4543 CD1 PHE C 126 76.857 50.374 20.293 1.000 22.75 ATOM 4544 CD2 PHE C 126 75.888 52.458 20.889 1.000 28.36 ATOM 4545 CE1 PHE C 126 76.083 50.328 19.149 1.000 17.53 ATOM 4546 CE2 PHE C 126 75.108 52.433 19.749 1.000 23.72 ATOM 4547 CE PHE C 126 75.205 51.364 18.876 1.000 21.00 ATOM 4548 C PHE C 126 79.066 53.322 21.541 1.000 23.15 ATOM 4549 O PHE C 126 79.013 53.494 20.317 1.000 21.11 ATOM 4550 N ASN C 127 79.106 54.356 22.373 1.000 18.49 ATOM 4551 CA ASN C 127 79.088 55.727 21.869 1.000 23.03 ATOM 4552 CE ASN C 127 79.101 56.743 23.008 1.000 21.45 ATOM 4553 CG ASN C 127 78.811 58.157 22.556 1.000 25.25 ATOM 4554 OD1 ASN C 127 78.014 58.378 21.642 1.000 29.13 ATOM 4555 ND2 ASN C 127 79.444 59.142 23.178 1.000 21.91 ATOM 4556 C ASN C 127 80.275 55.975 20.937 1.000 25.87 ATOM 4557 O ASN C 127 80.132 56.542 19.855 1.000 28.62 ATOM 4558 N VAL C 128 81.462 55.550 21.358 1.000 24.08 ATOM 4559 CA VAL C 128 82.651 55.701 20.526 1.000 21.95 ATOM 4560 CE VAL C 128 83.914 55.317 21.317 1.000 26.51 ATOM 4561 CD1 VAL C 128 85.134 55.394 20.406 1.000 22.25 ATOM 4562 CG2 VAL C 128 84.064 56.225 22.528 1.000 22.93 ATOM 4563 C VAL C 128 82.555 54.854 19.264 1.000 23.58 ATOM 4564 O VAL C 128 82.918 55.250 18.153 1.000 25.79 ATOM 4565 N ILE C 129 82.028 53.643 19.408 1.000 20.57 ATOM 4566 CA ILE C 129 81.911 52.748 18.263 1.000 20.61 ATOM 4567 CB ILE C 129 81.347 51.377 18.686 1.000 19.62 ATOM 4568 CG2 ILE C 129 80.846 50.638 17.458 1.000 17.68 ATOM 4569 CG1 ILE C 129 82.345 50.542 19.491 1.000 18.07 ATOM 4570 CD1 ILE C 129 81.885 49.185 19.946 1.000 14.79 ATOM 4571 C ILE C 129 81.046 53.324 17.151 1.000 25.58 ATOM 4572 O ILE C 129 81.456 53.326 15.982 1.000 24.80 ATOM 4573 N ARG C 130 79.849 53.789 17.487 1.000 22.22 ATOM 4574 CA ARG C 130 78.908 54.263 16.478 1.000 22.61 ATOM 4575 CB ARG C 130 77.534 54.507 17.124 1.000 24.83 ATOM 4576 CG ARG C 130 77.407 55.858 17.785 1.000 20.11 ATOM 4577 CG ARG C 130 76.273 56.001 18.789 1.000 22.05 ATOM 4578 NE ARG C 130 76.439 57.318 19.415 1.000 27.62 ATOM 4579 CZ ARG C 130 75.884 58.453 19.041 1.000 24.47 ATOM 4580 NE1 ARG C 130 76.165 59.557 19.720 1.000 23.28 ATOM 4581 NE2 ARG C 130 75.054 58.521 18.014 1.000 20.98 ATOM 4582 C ARG C 130 79.421 55.523 15.796 1.000 27.40 ATOM 4583 O ARG C 130 79.228 55.740 14.594 1.000 23.73 ATOM 4584 N LEU C 131 80.103 56.372 16.567 1.000 23.20 ATOM 4585 CA LEU C 131 80.646 57.606 16.013 1.000 26.88 ATOM 4586 CB LEU C 131 80.905 58.629 17.127 1.000 23.30 ATOM 4587 CG LEU C 131 79.654 59.282 17.728 1.000 28.73 ATOM 4588 CD1 LEU C 131 79.998 60.155 18.926 1.000 20.58 ATOM 4589 CD2 LEU C 131 78.925 60.105 16.673 1.000 33.54 ATOM 4590 C LEU C 131 81.917 57.344 15.213 1.000 29.94 ATOM 4591 O LEU C 131 82.072 57.881 14.115 1.000 25.36 ATOM 4592 N VAL C 132 82.834 56.531 15.740 1.000 22.06 ATOM 4593 CA VAL C 132 84.060 56.279 14.987 1.000 19.86 ATOM 4594 CB VAL C 132 85.144 55.586 15.823 1.000 20.83 ATOM 4595 CG1 VAL C 132 84.951 54.087 15.879 1.000 20.03 ATOM 4596 CG2 VAL C 132 86.517 55.930 15.238 1.000 23.88 ATOM 4597 C VAL C 132 83.760 55.452 13.735 1.000 22.63 ATOM 4598 O VAL C 132 84.474 55.583 12.735 1.000 26.93 ATOM 4599 N ALA C 133 82.711 54.633 13.750 1.000 16.38 ATOM 4600 CA ALA C 133 82.362 53.861 12.560 1.000 22.93 ATOM 4601 CB ALA C 133 81.248 52.865 12.849 1.000 23.49 ATOM 4602 C ALA C 133 81.967 54.783 11.408 1.000 25.68 ATOM 4603 O ALA C 133 82.304 54.533 10.248 1.000 25.79 ATOM 4604 N GLY C 134 81.258 55.870 11.697 1.000 26.27 ATOM 4605 CA GLY C 134 80.967 56.883 10.693 1.000 29.86 ATOM 4606 C GLY C 134 82.235 57.527 10.168 1.000 35.29 ATOM 4607 O GLY C 134 82.350 57.894 8.995 1.000 32.90 ATOM 4608 N GLU C 135 83.254 57.680 11.022 1.000 33.22 ATOM 4609 CA GLU C 135 84.500 58.252 10.509 1.000 27.55 ATOM 4610 CE GLU C 135 85.392 58.749 11.645 1.000 27.14 ATOM 4611 CG GLU C 135 84.779 59.910 12.415 1.000 31.58 ATOM 4612 CD GLU C 135 84.524 61.133 11.549 1.000 34.25 ATOM 4613 OE1 GLU C 135 83.509 61.813 11.805 1.000 48.00 ATOM 4614 OE2 GLU C 135 85.313 61.402 10.623 1.000 44.39 ATOM 4615 C GLU C 135 85.249 57.245 9.654 1.000 27.65 ATOM 4616 O GLU C 135 85.776 57.596 8.595 1.000 31.08 ATOM 4617 N MET C 136 85.293 55.991 10.094 1.000 20.13 ATOM 4618 CA MET C 136 85.986 55.000 9.275 1.000 22.80 ATOM 4619 CB MET C 136 86.163 53.693 10.043 1.000 24.93 ATOM 4620 CG MET C 136 87.064 53.805 11.266 1.000 26.00 ATOM 4621 SD MET C 136 87.004 52.294 12.257 1.000 26.60 ATOM 4622 CE MET C 136 88.201 52.656 13.540 1.000 25.70 ATOM 4623 C MET C 136 85.225 54.755 7.978 1.000 21.26 ATOM 4624 O MET C 136 85.756 54.286 6.973 1.000 26.59 ATOM 4625 N GLY C 137 83.936 55.076 7.981 1.000 26.75 ATOM 4626 CA GLY C 137 83.143 54.888 6.766 1.000 31.17 ATOM 4627 C GLY C 137 83.660 55.747 5.622 1.000 33.76 ATOM 4628 O GLY C 137 83.484 35.416 4.447 1.000 32.88 ATOM 4629 N GLN C 138 84.303 56.859 5.974 1.000 27.37 ATOM 4630 CA GLN C 138 84.791 57.797 4.973 1.000 28.73 ATOM 4631 CE GLN C 138 84.859 59.194 5.578 1.000 32.69 ATOM 4632 C GLN C 138 86.141 57.384 4.411 1.000 32.99 ATOM 4633 O GLN C 138 86.671 58.018 3.497 1.000 36.53 ATOM 4634 N ASN C 139 86.745 56.324 4.942 1.000 31.67 ATOM 4635 CA ASN C 139 88.056 55.934 4.429 1.000 30.49 ATOM 4636 CE ASN C 139 88.847 55.085 5.419 1.000 31.45 ATOM 4637 CG ASN C 139 89.086 55.684 6.785 1.000 34.68 ATOM 4638 OD1 ASN C 139 89.055 56.894 7.000 1.000 33.74 ATOM 4639 ND2 ASN C 139 89.334 54.812 7.762 1.000 28.28 ATOM 4640 C ASN C 139 87.884 55.142 3.136 1.000 30.33 ATOM 4641 O ASN C 139 86.907 54.415 2.977 1.000 31.18 ATOM 4642 N GLU C 140 88.838 55.260 2.219 1.000 32.41 ATOM 4643 CA GLU C 140 88.838 54.364 1.063 1.000 33.47 ATOM 4644 CE GLU C 140 89.741 54.885 −0.038 1.000 36.95 ATOM 4645 C GLU C 140 89.274 52.976 1.528 1.000 33.19 ATOM 4646 O GLU C 140 90.249 52.875 2.283 1.000 30.54 ATOM 4647 N PRO C 141 88.575 51.929 1.111 1.000 30.85 ATOM 4648 CD PRO C 141 87.385 51.919 0.252 1.000 28.75 ATOM 4649 CA PRO C 141 88.970 50.578 1.528 1.000 31.41 ATOM 4650 CB PRO C 141 87.893 49.670 0.942 1.000 31.98 ATOM 4651 CG PRO C 141 86.781 50.569 0.534 1.000 33.28 ATOM 4652 C PRO C 141 90.330 50.204 0.948 1.000 37.57 ATOM 4653 O PRO C 141 90.625 50.524 −0.205 1.000 39.30 ATOM 4654 N ASP C 142 91.151 49.522 1.745 1.000 32.93 ATOM 4655 CA ASP C 142 92.444 49.095 1.212 1.000 31.17 ATOM 4656 CB ASP C 142 93.376 48.639 2.322 1.000 32.74 ATOM 4657 CG ASP C 142 92.888 47.444 3.108 1.000 34.79 ATOM 4658 OD1 ASP C 142 91.946 46.748 2.677 1.000 23.82 ATOM 4659 OD2 ASP C 142 93.479 47.192 4.185 1.000 36.00 ATOM 4660 C ASP C 142 92.223 47.986 0.182 1.000 35.49 ATOM 4661 O ASP C 142 91.079 47.730 −0.205 1.000 28.21 ATOM 4662 N GLN C 143 93.321 47.372 −0.234 1.000 34.68 ATOM 4663 CA GLN C 143 93.292 46.328 −1.248 1.000 38.05 ATOM 4664 CE GLN C 143 94.716 45.927 −1.617 1.000 37.56 ATOM 4665 C GLN C 143 92.502 45.115 −0.776 1.000 39.79 ATOM 4666 O GLN C 143 92.057 44.304 −1.596 1.000 39.29 ATOM 4667 N GLY C 144 92.336 44.982 0.539 1.000 34.34 ATOM 4668 CA GLY C 144 91.609 43.857 1.105 1.000 30.14 ATOM 4669 C GLY C 144 90.163 44.224 1.396 1.000 30.98 ATOM 4670 O GLY C 144 89.417 43.410 1.939 1.000 33.23 ATOM 4671 N GLY C 145 89.767 45.439 1.035 1.000 28.94 ATOM 4672 CA GLY C 145 88.407 45.893 1.253 1.000 24.37 ATOM 4673 C GLY C 145 88.236 46.543 2.603 1.000 26.97 ATOM 4674 O GLY C 145 87.132 46.942 2.981 1.000 25.24 ATOM 4675 N GLN C 146 89.310 46.676 3.378 1.000 28.50 ATOM 4676 CA GLN C 146 89.168 47.169 4.746 1.000 27.93 ATOM 4677 CE GLN C 146 90.248 46.534 5.635 1.000 27.83 ATOM 4678 CG GLN C 146 89.994 46.739 7.126 1.000 30.00 ATOM 4679 CD GLN C 146 90.976 45.937 7.966 1.000 29.61 ATOM 4680 OE1 GLN C 146 90.812 44.731 8.172 1.000 27.76 ATOM 4681 NE2 GLN C 146 92.007 46.631 8.437 1.000 24.62 ATOM 4682 C GLN C 146 89.249 48.685 4.869 1.000 27.94 ATOM 4683 O GLN C 146 90.091 49.343 4.260 1.000 30.22 ATOM 4684 N ARG C 147 88.364 49.237 5.689 1.000 22.37 ATOM 4685 CA ARG C 147 88.337 50.649 6.015 1.000 21.86 ATOM 4686 CE ARG C 147 86.936 51.211 5.751 1.000 21.94 ATOM 4687 CG ARG C 147 86.559 51.337 4.277 1.000 23.66 ATOM 4688 CD ARG C 147 85.272 52.142 4.189 1.000 28.50 ATOM 4689 NE ARG C 147 84.833 52.483 2.843 1.000 29.48 ATOM 4690 CZ ARG C 147 83.997 51.726 2.144 1.000 30.36 ATOM 4691 NE1 ARG C 147 83.625 52.086 0.927 1.000 40.21 ATOM 4692 NH2 ARG C 147 83.528 50.599 2.656 1.000 30.57 ATOM 4693 C ARG C 147 88.704 50.934 7.468 1.000 23.83 ATOM 4694 O ARG C 147 89.023 52.084 7.799 1.000 21.61 ATOM 4695 N GLY C 148 88.657 49.944 8.359 1.000 23.27 ATOM 4696 CA GLY C 148 88.977 50.241 9.754 1.000 22.95 ATOM 4697 C GLY C 148 88.910 49.030 10.663 1.000 23.86 ATOM 4698 O GLY C 148 88.404 47.983 10.263 1.000 23.15 ATOM 4699 N VAL C 149 89.433 49.170 11.880 1.000 21.41 ATOM 4700 CA VAL C 149 89.438 48.111 12.873 1.000 21.07 ATOM 4701 CB VAL C 149 90.815 47.434 13.047 1.000 24.01 ATOM 4702 CG1 VAL C 149 90.663 46.155 13.860 1.000 25.18 ATOM 4703 CG2 VAL C 149 91.461 47.147 11.702 1.000 31.46 ATOM 4704 C VAL C 149 89.015 48.660 14.236 1.000 21.87 ATOM 4705 O VAL C 149 89.573 49.650 14.719 1.000 22.20 ATOM 4706 N ILE C 150 88.036 48.009 14.854 1.000 21.29 ATOM 4707 CA ILE C 150 87.581 48.459 16.177 1.000 22.11 ATOM 4708 CB ILE C 150 86.120 48.928 16.138 1.000 23.77 ATOM 4709 CG2 ILE C 150 85.599 49.309 17.516 1.000 22.27 ATOM 4710 CG1 ILE C 150 85.895 50.080 15.154 1.000 22.12 ATOM 4711 CD1 ILE C 150 84.436 50.412 14.925 1.000 22.79 ATOM 4712 C ILE C 150 87.781 47.333 17.185 1.000 21.41 ATOM 4713 O ILE C 150 87.392 46.194 16.955 1.000 23.38 ATOM 4714 N ILE C 151 88.421 47.652 18.294 1.000 20.58 ATOM 4715 CA ILE C 151 88.771 46.712 19.354 1.000 21.20 ATOM 4716 CB ILE C 151 90.297 46.547 19.456 1.000 19.12 ATOM 4717 CG2 ILE C 151 90.718 45.602 20.566 1.000 16.71 ATOM 4718 CG1 ILE C 151 90.934 46.101 18.134 1.000 24.71 ATOM 4719 CD1 ILE C 151 92.445 46.052 18.169 1.000 24.82 ATOM 4720 C ILE C 151 88.203 47.214 20.680 1.000 21.43 ATOM 4721 O ILE C 151 88.441 48.370 21.032 1.000 23.16 ATOM 4722 N ASN C 152 87.456 46.374 21.384 1.000 19.89 ATOM 4723 CA ASN C 152 86.858 46.780 22.658 1.000 20.31 ATOM 4724 CB ASN C 152 85.338 46.577 22.645 1.000 18.41 ATOM 4725 CG ASN C 152 84.762 47.031 21.311 1.000 17.45 ATOM 4726 OD1 ASN C 152 84.199 46.232 20.564 1.000 34.00 ATOM 4727 ND2 ASN C 152 84.929 48.310 21.028 1.000 15.97 ATOM 4728 C ASN C 152 87.458 45.995 23.816 1.000 22.13 ATOM 4729 O ASN C 152 88.053 44.942 23.593 1.000 19.05 ATOM 4730 N THR C 153 87.298 46.505 25.036 1.000 22.52 ATOM 4731 CA THR C 153 87.802 45.768 26.192 1.000 19.48 ATOM 4732 CB THR C 153 88.770 46.586 27.056 1.000 19.67 ATOM 4733 OG1 THR C 153 89.765 47.237 26.247 1.000 20.53 ATOM 4734 CG2 THR C 153 89.519 45.635 27.984 1.000 18.55 ATOM 4735 C THR C 153 86.647 45.286 27.065 1.000 19.43 ATOM 4736 O THR C 153 85.923 46.104 27.629 1.000 19.18 ATOM 4737 N ALA C 154 86.504 43.967 27.145 1.000 17.96 ATOM 4738 CA ALA C 154 85.546 43.388 28.091 1.000 23.21 ATOM 4739 CB ALA C 154 84.783 42.231 27.479 1.000 16.13 ATOM 4740 C ALA C 154 86.313 42.982 29.354 1.000 17.34 ATOM 4741 O ALA C 154 87.034 43.830 29.893 1.000 20.75 ATOM 4742 N SER C 155 86.155 41.747 29.783 1.000 20.86 ATOM 4743 CA SER C 155 86.764 41.215 30.997 1.000 18.50 ATOM 4744 CB SER C 155 86.326 42.008 32.231 1.000 20.65 ATOM 4745 OG SER C 155 86.621 41.304 33.431 1.000 19.32 ATOM 4746 CB SER C 155 86.363 39.764 31.180 1.000 18.55 ATOM 4747 O SER C 155 85.277 39.408 30.715 1.000 17.19 ATOM 4748 N VAL C 156 87.165 38.924 31.847 1.000 17.22 ATOM 4749 CA VAL C 156 86.673 37.573 32.114 1.000 17.81 ATOM 4750 CB VAL C 156 87.760 36.650 32.704 1.000 22.90 ATOM 4751 CG1 VAL C 156 88.915 36.479 31.725 1.000 24.56 ATOM 4752 CG2 VAL C 156 88.283 37.194 34.019 1.000 22.39 ATOM 4753 C VAL C 156 85.464 37.589 33.060 1.000 15.91 ATOM 4754 O VAL C 156 84.755 36.586 33.186 1.000 18.83 ATOM 4755 N ALA C 157 85.215 38.704 33.730 1.000 15.01 ATOM 4756 CA ALA C 157 84.041 38.914 34.563 1.000 14.91 ATOM 4757 CB ALA C 157 84.140 40.284 35.218 1.000 13.46 ATOM 4758 C ALA C 157 82.748 38.820 33.761 1.000 23.2.4 ATOM 4759 O ALA C 157 81.685 38.651 34.360 1.000 22.64 ATOM 4760 N ALA C 158 82.854 38.929 32.432 1.000 19.67 ATOM 4761 CA ALA C 158 81.729 38.712 31.540 1.000 20.27 ATOM 4762 CB ALA C 158 82.059 39.109 30.107 1.000 20.82 ATOM 4763 C ALA C 158 81.304 37.253 31.572 1.000 20.48 ATOM 4764 O ALA C 158 80.159 36.916 31.264 1.000 22.01 ATOM 4765 N PHE C 159 82.244 36.380 31.953 1.000 17.98 ATOM 4766 CA PHE C 159 81.928 34.952 31.954 1.000 21.05 ATOM 4767 CB PHE C 159 82.917 34.205 31.056 1.000 22.40 ATOM 4768 CG PHE C 159 83.083 34.828 29.675 1.000 24.42 ATOM 4769 CD1 PHE C 159 84.241 35.502 29.325 1.000 21.89 ATOM 4770 CD2 PHE C 159 82.056 34.719 28.749 1.000 25.13 ATOM 4771 CE1 PHE C 159 84.378 36.056 28.058 1.000 23.61 ATOM 4772 CE2 PHE C 159 82.192 35.266 27.481 1.000 25.88 ATOM 4773 CZ PHE C 159 83.350 35.932 27.140 1.000 19.73 ATOM 4774 C PHE C 159 81.926 34.345 33.358 1.000 25.32 ATOM 4775 O PHE C 159 81.134 33.437 33.625 1.000 24.04 ATOM 4776 N GLU C 160 82.779 34.802 34.258 1.000 21.14 ATOM 4777 CA GLU C 160 82.875 34.281 35.615 1.000 24.99 ATOM 4778 CE GLU C 160 84.158 33.484 35.857 1.000 25.61 ATOM 4779 CG GLU C 160 84.429 32.284 34.995 1.000 30.25 ATOM 4780 CD GLU C 160 85.521 32.475 33.964 1.000 32.66 ATOM 4781 OE1 GLU C 160 85.262 32.081 32.809 1.000 32.29 ATOM 4782 OE2 GLU C 160 86.617 33.001 34.246 1.000 22.74 ATOM 4783 C GLU C 160 82.864 35.434 36.624 1.000 22.02 ATOM 4784 O GLU C 160 83.791 35.528 37.437 1.000 21.01 ATOM 4785 N GLY C 161 81.866 36.304 36.567 1.000 17.29 ATOM 4786 CA GLY C 161 81.851 37.439 37.491 1.000 19.00 ATOM 4787 C GLY C 161 81.868 36.907 38.928 1.000 20.23 ATOM 4788 O GLY C 161 81.181 35.925 39.227 1.000 17.32 ATOM 4789 N GLN C 162 82.649 37.541 39.781 1.000 18.84 ATOM 4790 CA GLN C 162 82.813 37.127 41.171 1.000 22.71 ATOM 4791 CE GLN C 162 84.206 37.487 41.685 1.000 21.68 ATOM 4792 CG GLN C 162 85.379 36.970 40.862 1.000 23.66 ATOM 4793 CD GLN C 162 86.694 37.252 41.577 1.000 24.38 ATOM 4794 OE1 GLN C 162 87.191 38.376 41.561 1.000 25.66 ATOM 4795 NE2 GLN C 162 87.262 36.237 42.215 1.000 22.36 ATOM 4796 C GLN C 162 81.789 37.808 42.070 1.000 23.11 ATOM 4797 O GLN C 162 81.098 38.733 41.640 1.000 21.46 ATOM 4798 N VAL C 163 81.711 37.370 43.324 1.000 24.81 ATOM 4799 CA VAL C 163 80.852 38.059 44.290 1.000 21.14 ATOM 4800 CE VAL C 163 80.982 37.467 45.699 1.000 18.37 ATOM 4801 CG1 VAL C 163 80.299 38.340 46.731 1.000 22.10 ATOM 4802 CG2 VAL C 163 80.409 36.053 45.714 1.000 14.21 ATOM 4803 C VAL C 163 81.224 39.537 44.312 1.000 23.76 ATOM 4804 O VAL C 163 82.409 39.853 44.407 1.000 25.31 ATOM 4805 N GLY C 164 80.234 40.420 44.203 1.000 19.76 ATOM 4806 CA GLY C 164 80.469 41.844 44.194 1.000 18.89 ATOM 4807 C GLY C 164 80.568 42.442 42.804 1.000 23.71 ATOM 4808 O GLY C 164 80.662 43.669 42.678 1.000 25.11 ATOM 4809 N GLN C 165 80.556 41.604 41.775 1.000 19.10 ATOM 4810 CA GLN C 165 80.814 42.018 40.411 1.000 23.28 ATOM 4811 CB GLN C 165 81.804 41.016 39.777 1.000 21.58 ATOM 4812 CG GLN C 165 83.259 41.287 40.143 1.000 24.62 ATOM 4813 CD GLN C 165 84.213 40.621 39.167 1.000 25.83 ATOM 4814 OE1 GLN C 165 84.081 39.433 38.878 1.000 23.28 ATOM 4815 NE2 GLN C 165 85.168 41.380 38.658 1.000 24.36 ATOM 4816 C GLN C 165 79.596 42.094 39.507 1.000 25.66 ATOM 4817 O GLN C 165 79.767 42.167 38.281 1.000 22.34 ATOM 4818 N ALA C 166 78.382 42.080 40.032 1.000 19.52 ATOM 4819 CA ALA C 166 77.190 42.135 39.191 1.000 19.44 ATOM 4820 CB ALA C 166 75.942 42.227 40.065 1.000 21.99 ATOM 4821 C ALA C 166 77.195 43.288 38.199 1.000 22.65 ATOM 4822 O ALA C 166 76.961 43.089 37.001 1.000 24.51 ATOM 4823 N ALA C 167 77.441 44.520 38.631 1.000 18.71 ATOM 4824 CA ALA C 167 77.378 45.643 37.693 1.000 19.62 ATOM 4825 CE ALA C 167 77.455 46.966 38.438 1.000 19.07 ATOM 4826 C ALA C 167 78.485 45.553 36.648 1.000 23.28 ATOM 4827 O ALA C 167 78.252 45.719 35.448 1.000 21.18 ATOM 4828 N TYR C 168 79.709 45.290 37.101 1.000 19.90 ATOM 4829 CA TYR C 168 80.830 45.168 36.171 1.000 18.57 ATOM 4830 CE TYR C 168 82.120 44.873 36.916 1.000 20.89 ATOM 4831 CG TYR C 168 83.408 45.040 36.139 1.000 19.26 ATOM 4832 CD1 TYR C 168 83.852 46.293 35.737 1.000 19.37 ATOM 4833 CE1 TYR C 168 85.030 46.461 35.030 1.000 18.00 ATOM 4834 CD2 TYR C 168 84.195 43.936 35.814 1.000 16.76 ATOM 4835 CE2 TYR C 168 85.379 44.090 35.105 1.000 17.87 ATOM 4836 CZ TYR C 168 85.783 45.348 34.717 1.000 21.43 ATOM 4837 OH TYR C 168 86.957 45.507 34.022 1.000 20.56 ATOM 4838 C TYR C 168 80.528 44.073 35.155 1.000 21.19 ATOM 4839 O TYR C 168 80.721 44.258 33.956 1.000 23.83 ATOM 4840 N SER C 169 80.037 42.938 35.647 1.000 20.45 ATOM 4841 CA SER C 169 79.751 41.804 34.780 1.000 17.69 ATOM 4842 CB SER C 169 79.316 40.582 35.587 1.000 17.03 ATOM 4843 OG SER C 169 80.453 39.915 36.117 1.000 19.86 ATOM 4844 CB SER C 169 78.692 42.157 33.741 1.000 24.37 ATOM 4845 O SER C 169 78.810 41.724 32.586 1.000 24.38 ATOM 4846 N ALA C 170 77.682 42.920 34.151 1.000 22.07 ATOM 4847 CA ALA C 170 76.612 43.285 33.214 1.000 18.30 ATOM 4848 CE ALA C 170 75.502 44.022 33.939 1.000 16.49 ATOM 4849 C ALA C 170 77.189 44.135 32.089 1.000 22.43 ATOM 4850 O ALA C 170 76.948 43.962 30.898 1.000 22.50 ATOM 4851 N SER C 171 78.009 45.113 32.495 1.000 20.04 ATOM 4852 CA SER C 171 78.564 46.029 31.503 1.000 18.05 ATOM 4853 CE SER C 171 79.284 47.187 32.185 1.000 18.91 ATOM 4854 OG SER C 171 80.590 46.838 32.608 1.000 22.61 ATOM 4855 CB SER C 171 79.486 45.276 30.547 1.000 21.94 ATOM 4856 O SER C 171 79.442 45.523 29.341 1.000 24.60 ATOM 4857 N LYS C 172 80.310 44.365 31.066 1.000 15.08 ATOM 4858 CA LYS C 172 81.277 43.690 30.207 1.000 19.64 ATOM 4859 CB LYS C 172 82.467 43.186 31.026 1.000 19.41 ATOM 4860 CG LYS C 172 83.239 44.295 31.722 1.000 16.40 ATOM 4861 CD LYS C 172 83.739 45.356 30.767 1.000 21.19 ATOM 4862 CE LYS C 172 84.930 46.123 31.313 1.000 16.40 ATOM 4863 NZ LYS C 172 85.562 47.002 30.286 1.000 17.94 ATOM 4864 G LYS C 172 80.621 42.556 29.427 1.000 23.18 ATOM 4865 O LYS C 172 81.032 42.214 28.313 1.000 20.83 ATOM 4866 N GLY C 173 79.574 41.964 29.995 1.000 19.64 ATOM 4867 CA GLY C 173 78.793 40.984 29.258 1.000 16.61 ATOM 4868 C GLY C 173 78.080 41.671 28.099 1.000 20.08 ATOM 4869 O GLY C 173 77.848 41.054 27.062 1.000 19.57 ATOM 4870 N GLY C 174 77.738 42.944 28.280 1.000 19.74 ATOM 4871 CA GLY C 174 77.081 43.697 27.218 1.000 18.27 ATOM 4872 C GLY C 174 78.045 43.907 26.056 1.000 23.73 ATOM 4873 O GLY C 174 77.672 43.840 24.882 1.000 19.78 ATOM 4874 N ILE C 175 79.303 44.172 26.389 1.000 23.27 ATOM 4875 CA ILE C 175 80.330 44.337 25.365 1.000 20.71 ATOM 4876 CE ILE C 175 81.688 44.695 25.994 1.000 23.26 ATOM 4877 CG2 ILE C 175 82.770 44.772 24.926 1.000 20.37 ATOM 4878 CG1 ILE C 175 81.688 45.982 26.829 1.000 21.73 ATOM 4879 CD1 ILE C 175 81.456 47.221 25.992 1.000 30.34 ATOM 4880 C ILE C 175 80.487 43.065 24.541 1.000 20.73 ATOM 4881 O ILE C 175 80.526 43.084 23.313 1.000 23.88 ATOM 4882 N VAL C 176 80.585 41.936 25.239 1.000 15.48 ATOM 4883 CA VAL C 176 80.725 40.651 24.573 1.000 14.04 ATOM 4884 CB VAL C 176 80.845 39.518 25.610 1.000 19.74 ATOM 4885 CG1 VAL C 176 80.575 38.161 24.987 1.000 18.87 ATOM 4886 CG2 VAL C 176 82.226 39.560 26.249 1.000 19.59 ATOM 4887 C VAL C 176 79.539 40.390 23.660 1.000 20.41 ATOM 4888 O VAL C 176 79.680 40.023 22.493 1.000 20.54 ATOM 4889 N GLY C 177 78.334 40.569 24.193 1.000 19.61 ATOM 4890 CA GLY C 177 77.136 40.316 23.424 1.000 16.92 ATOM 4891 C GLY C 177 76.986 41.203 22.213 1.000 21.30 ATOM 4892 O GLY C 177 76.382 40.812 21.208 1.000 24.01 ATOM 4893 N MET C 178 77.496 42.432 22.215 1.000 19.61 ATOM 4894 CA MET C 178 77.233 43.272 21.046 1.000 17.86 ATOM 4895 CB MET C 178 76.979 44.720 21.454 1.000 17.13 ATOM 4896 CG MET C 178 78.191 45.421 22.045 1.000 21.09 ATOM 4897 SD MET C 178 77.817 47.098 22.590 1.000 24.03 ATOM 4898 CE MET C 178 79.476 47.732 22.850 1.000 18.90 ATOM 4899 C MET C 178 78.374 43.192 20.039 1.000 21.69 ATOM 4900 O MET C 178 78.306 43.821 18.980 1.000 22.15 ATOM 4901 N THR C 179 79.413 42.419 20.350 1.000 18.49 ATOM 4902 CA THR C 179 80.552 42.343 19.435 1.000 19.38 ATOM 4903 CB THR C 179 81.715 41.578 20.077 1.000 18.75 ATOM 4904 OG1 THR C 179 82.308 42.431 21.076 1.000 18.08 ATOM 4905 CG2 THR C 179 82.821 41.290 19.072 1.000 15.74 ATOM 4906 C THR C 179 80.138 41.746 18.094 1.000 23.48 ATOM 4907 O THR C 179 80.402 42.366 17.054 1.000 20.76 ATOM 4908 N LEU C 180 79.481 40.588 18.052 1.000 19.56 ATOM 4909 CA LEU C 180 79.110 39.991 16.771 1.000 17.92 ATOM 4910 CE LEU C 180 78.526 38.592 16.974 1.000 18.98 ATOM 4911 CG LEU C 180 78.152 37.823 15.702 1.000 24.14 ATOM 4912 CD1 LEU C 180 79.365 37.659 14.797 1.000 26.21 ATOM 4913 CD2 LEU C 180 77.569 36.461 16.040 1.000 20.39 ATOM 4914 C LEU C 180 78.122 40.839 15.977 1.000 21.92 ATOM 4915 O LEU C 180 78.396 41.090 14.788 1.000 22.82 ATOM 4916 N PRO C 181 77.001 41.271 16.543 1.000 21.19 ATOM 4917 CD PRO C 181 76.478 41.009 17.891 1.000 20.31 ATOM 4918 CA PRO C 181 76.067 42.119 15.783 1.000 23.54 ATOM 4919 CB PRO C 181 74.987 42.531 16.795 1.000 22.69 ATOM 4920 CG PRO C 181 75.557 42.179 18.132 1.000 19.47 ATOM 4921 C PRO C 181 76.735 43.365 15.219 1.000 25.60 ATOM 4922 O PRO C 181 76.450 43.782 14.095 1.000 20.77 ATOM 4923 N ILE C 182 77.631 44.003 15.963 1.000 20.42 ATOM 4924 CA ILE C 182 78.267 45.199 15.389 1.000 17.66 ATOM 4925 CE ILE C 182 78.947 46.036 16.481 1.000 16.77 ATOM 4926 CG2 ILE C 182 79.697 47.205 15.870 1.000 18.19 ATOM 4927 CG1 ILE C 182 77.971 46.528 17.557 1.000 18.40 ATOM 4928 CD1 ILE C 182 78.654 47.095 18.788 1.000 21.84 ATOM 4929 C ILE C 182 79.230 44.797 14.285 1.000 23.52 ATOM 4930 O ILE C 182 79.357 45.488 13.268 1.000 23.23 ATOM 4931 N ALA C 183 79.919 43.670 14.421 1.000 21.40 ATOM 4932 CA ALA C 183 80.709 43.151 13.304 1.000 21.08 ATOM 4933 CB ALA C 183 81.451 41.870 13.661 1.000 20.13 ATOM 4934 C ALA C 183 79.796 42.897 12.108 1.000 24.15 ATOM 4935 O ALA C 183 80.139 43.202 10.963 1.000 21.19 ATOM 4936 N ARG C 184 78.613 42.333 12.359 1.000 21.19 ATOM 4937 CA ARG C 184 77.712 42.082 11.228 1.000 22.02 ATOM 4938 CB ARG C 184 76.515 41.222 11.642 1.000 17.02 ATOM 4939 CG ARG C 184 76.907 39.790 11.944 1.000 16.66 ATOM 4940 CD ARG C 184 75.783 38.999 12.591 1.000 16.59 ATOM 4941 NE ARG C 184 76.015 37.569 12.471 1.000 18.43 ATOM 4942 CZ ARG C 184 75.293 36.593 12.985 1.000 18.80 ATOM 4943 NH1 ARG C 184 75.632 35.331 12.776 1.000 18.86 ATOM 4944 NH2 ARG C 184 74.219 36.873 13.715 1.000 21.57 ATOM 4945 C ARG C 184 77.259 43.401 10.614 1.000 21.95 ATOM 4946 O ARG C 184 77.243 43.521 9.383 1.000 21.48 ATOM 4947 N ASP C 185 76.913 44.384 11.444 1.000 15.88 ATOM 4948 CA ASP C 185 76.477 45.675 10.916 1.000 19.50 ATOM 4949 CB ASP C 185 76.280 46.734 11.997 1.000 19.32 ATOM 4950 CG ASP C 185 75.036 46.630 12.843 1.000 23.51 ATOM 4951 OD1 ASP C 185 75.002 47.321 13.882 1.000 23.02 ATOM 4952 OD2 ASP C 185 74.096 45.882 12.515 1.000 16.66 ATOM 4953 C ASP C 185 77.502 46.249 9.930 1.000 24.98 ATOM 4954 O ASP C 185 77.166 46.681 8.832 1.000 20.75 ATOM 4955 N LEU C 186 78.763 46.257 10.344 1.000 18.62 ATOM 4956 CA LEU C 186 79.810 46.982 9.640 1.000 20.87 ATOM 4957 CB LEU C 186 80.820 47.496 10.677 1.000 19.42 ATOM 4958 CG LEU C 186 80.255 48.395 11.775 1.000 22.20 ATOM 4959 CD1 LEU C 186 81.361 48.953 12.672 1.000 17.85 ATOM 4960 CD2 LEU C 186 79.458 49.547 11.178 1.000 21.31 ATOM 4961 C LEU C 186 80.528 46.154 8.586 1.000 21.49 ATOM 4962 O LEU C 186 81.397 46.655 7.861 1.000 23.84 ATOM 4963 N ALA C 187 80.183 44.878 8.511 1.000 14.05 ATOM 4964 CA ALA C 187 80.825 43.985 7.554 1.000 17.54 ATOM 4965 CB ALA C 187 80.217 42.594 7.650 1.000 15.77 ATOM 4966 C ALA C 187 80.757 44.492 6.117 1.000 23.42 ATOM 4967 O ALA C 187 81.804 44.388 5.460 1.000 24.58 ATOM 4968 N PRO C 188 79.646 44.987 5.594 1.000 26.75 ATOM 4969 CD PRO C 188 78.301 45.092 6.198 1.000 31.00 ATOM 4970 CA PRO C 188 79.633 45.490 4.212 1.000 26.89 ATOM 4971 CB PRO C 188 78.166 45.866 3.952 1.000 26.16 ATOM 4972 CG PRO C 188 77.395 45.132 4.995 1.000 31.72 ATOM 4973 C PRO C 188 80.485 46.730 4.014 1.000 31.65 ATOM 4974 O PRO C 188 80.776 47.121 2.878 1.000 33.18 ATOM 4975 N ILE C 189 80.914 47.408 5.076 1.000 26.20 ATOM 4976 CA ILE C 189 81.786 48.555 4.792 1.000 27.86 ATOM 4977 CE ILE C 189 81.251 49.840 5.440 1.000 33.18 ATOM 4978 CG2 ILE C 189 80.027 50.313 4.657 1.000 37.79 ATOM 4979 CG1 ILE C 189 80.947 49.727 6.931 1.000 28.57 ATOM 4980 CD1 ILE C 189 80.160 50.922 7.453 1.000 30.62 ATOM 4981 C ILE C 189 83.220 48.297 5.238 1.000 23.24 ATOM 4982 O ILE C 189 84.030 49.216 5.327 1.000 23.19 ATOM 4983 N GLY C 190 83.524 47.029 5.501 1.000 19.61 ATOM 4984 CA GLY C 190 84.877 46.607 5.781 1.000 21.76 ATOM 4985 C GLY C 190 85.479 47.116 7.065 1.000 23.87 ATOM 4986 O GLY C 190 86.657 47.460 7.125 1.000 24.45 ATOM 4987 N ILE C 191 84.685 47.169 8.138 1.000 23.04 ATOM 4988 CA ILE C 191 85.276 47.514 9.433 1.000 21.87 ATOM 4989 CE ILE C 191 84.574 48.715 10.074 1.000 20.61 ATOM 4990 CG2 ILE C 191 85.197 49.005 11.436 1.000 24.73 ATOM 4991 CG1 ILE C 191 84.550 49.983 9.218 1.000 20.90 ATOM 4992 CD1 ILE C 191 83.650 51.064 9.783 1.000 19.84 ATOM 4993 C ILE C 191 85.201 46.304 10.363 1.000 24.63 ATOM 4994 O ILE C 191 84.091 45.842 10.665 1.000 26.08 ATOM 4995 N ARG C 192 86.344 45.779 10.794 1.000 20.62 ATOM 4996 CA ARG C 192 86.350 44.608 11.674 1.000 21.27 ATOM 4997 CB ARG C 192 87.679 43.852 11.626 1.000 20.62 ATOM 4998 CG ARG C 192 87.985 43.203 10.285 1.000 20.90 ATOM 4999 CD ARG C 192 89.210 42.323 10.330 1.000 18.84 ATOM 5000 NE ARG C 192 90.478 43.041 10.348 1.000 23.01 ATOM 5001 CZ ARG C 192 91.355 43.045 11.346 1.000 22.55 ATOM 5002 NE1 ARG C 192 91.114 42.367 12.458 1.000 22.22 ATOM 5003 NH2 ARG C 192 92.487 43.730 11.251 1.000 20.98 ATOM 5004 C ARG C 192 86.057 45.037 13.114 1.000 20.57 ATOM 5005 O ARG C 192 86.400 46.163 13.482 1.000 20.36 ATOM 5006 N VAL C 193 85.419 44.161 13.885 1.000 20.86 ATOM 5007 CA VAL C 193 85.130 44.469 15.292 1.000 23.25 ATOM 5008 CE VAL C 193 83.659 44.842 15.515 1.000 23.85 ATOM 5009 CG1 VAL C 193 83.404 45.258 16.960 1.000 21.43 ATOM 5010 CG2 VAL C 193 83.258 45.976 14.575 1.000 18.16 ATOM 5011 C VAL C 193 85.519 43.281 16.170 1.000 20.12 ATOM 5012 O VAL C 193 85.008 42.175 15.996 1.000 16.74 ATOM 5013 N MET C 194 86.437 43.515 17.099 1.000 18.39 ATOM 5014 CA MET C 194 86.997 42.465 17.942 1.000 19.21 ATOM 5015 CB MET C 194 88.421 42.135 17.486 1.000 22.24 ATOM 5016 CG MET C 194 88.499 41.328 16.192 1.000 19.86 ATOM 5017 SD MET C 194 88.078 39.591 16.432 1.000 19.40 ATOM 5018 CE MET C 194 89.322 39.131 17.648 1.000 17.87 ATOM 5019 C MET C 194 87.013 42.862 19.415 1.000 21.78 ATOM 5020 O MET C 194 87.041 44.030 19.794 1.000 18.51 ATOM 5021 N THR C 195 87.010 41.871 20.302 1.000 20.94 ATOM 5022 CA THR C 195 87.027 42.216 21.729 1.000 20.90 ATOM 5023 CB THR C 195 85.629 41.984 22.337 1.000 22.49 ATOM 5024 OG1 THR C 195 84.713 42.952 21.794 1.000 19.71 ATOM 5025 CG2 THR C 195 85.641 42.176 23.843 1.000 20.67 ATOM 5026 C THR C 195 88.067 41.404 22.478 1.000 18.58 ATOM 5027 O THR C 195 88.280 40.218 22.235 1.000 21.52 ATOM 5028 N THR C 196 88.758 42.057 23.410 1.000 21.00 ATOM 5029 CA ILE C 196 89.699 41.346 24.271 1.000 20.59 ATOM 5030 CE ILE C 196 91.080 42.016 24.288 1.000 22.02 ATOM 5031 CG2 ILE C 196 91.954 41.401 25.365 1.000 13.39 ATOM 5032 CG1 ILE C 196 91.783 42.010 22.923 1.000 17.94 ATOM 5033 CD ILE C 196 92.835 43.078 22.761 1.000 17.09 ATOM 5034 C ILE C 196 89.116 41.295 25.687 1.000 17.92 ATOM 5035 O ILE C 196 88.617 42.327 26.135 1.000 18.00 ATOM 5036 N ALA C 197 89.174 40.135 26.328 1.000 17.64 ATOM 5037 CA ALA C 197 88.730 40.004 27.714 1.000 19.48 ATOM 5038 CE ALA C 197 87.709 38.893 27.885 1.000 15.55 ATOM 5039 C ALA C 197 89.935 39.750 28.611 1.000 17.38 ATOM 5040 O ALA C 197 90.373 38.612 28.764 1.000 21.58 ATOM 5041 N PRO C 198 90.505 40.791 29.198 1.000 14.98 ATOM 5042 CD PRO C 198 90.131 42.210 29.075 1.000 14.59 ATOM 5043 CA PRO C 198 91.655 40.584 30.080 1.000 16.28 ATOM 5044 CE PRO C 198 92.103 42.012 30.398 1.000 17.97 ATOM 5045 CG PRO C 198 91.423 42.907 29.412 1.000 14.71 ATOM 5046 C PRO C 198 91.249 39.874 31.368 1.000 20.85 ATOM 5047 O PRO C 198 90.121 40.024 31.837 1.000 20.67 ATOM 5048 N GLY C 199 92.145 39.101 31.962 1.000 18.62 ATOM 5049 CA GLY C 199 91.876 38.524 33.287 1.000 20.40 ATOM 5050 C GLY C 199 92.267 39.544 34.351 1.000 24.59 ATOM 5051 O GLY C 199 91.475 40.429 34.678 1.000 27.81 ATOM 5052 N LEU C 200 93.486 39.442 34.871 1.000 22.82 ATOM 5053 CA LEU C 200 93.987 40.368 35.882 1.000 23.36 ATOM 5054 CE LEU C 200 94.232 39.641 37.207 1.000 28.78 ATOM 5055 CG LEU C 200 93.115 38.748 37.751 1.000 28.91 ATOM 5056 CD1 LEU C 200 93.669 37.767 38.771 1.000 25.33 ATOM 5057 CD2 LEU C 200 92.004 39.596 38.359 1.000 26.21 ATOM 5058 C LEU C 200 95.284 41.027 35.427 1.000 22.30 ATOM 5059 O LEU C 200 96.275 40.332 35.157 1.000 26.10 ATOM 5060 N PHE C 201 95.300 42.353 35.329 1.000 18.24 ATOM 5061 CA PHE C 201 96.485 43.048 34.842 1.000 21.20 ATOM 5062 CB PHE C 201 96.197 43.708 33.490 1.000 20.11 ATOM 5063 CG PHE C 201 96.364 42.761 32.305 1.000 22.13 ATOM 5064 CD1 PHE C 201 95.433 41.770 32.063 1.000 20.96 ATOM 5065 CD2 PHE C 201 97.455 42.886 31.460 1.000 21.03 ATOM 5066 CE1 PHE C 201 95.583 40.920 30.980 1.000 21.62 ATOM 5067 CE2 PHE C 201 97.605 42.044 30.374 1.000 22.29 ATOM 5068 CZ PHE C 201 96.666 41.062 30.134 1.000 15.56 ATOM 5069 C PHE C 201 96.955 44.125 35.813 1.000 24.21 ATOM 5070 O PHE C 201 96.132 44.768 36.461 1.000 26.00 ATOM 5071 N GLY C 202 98.265 44.325 35.892 1.000 25.77 ATOM 5072 CA GLY C 202 98.844 45.302 36.792 1.000 26.53 ATOM 5073 C GLY C 202 98.711 46.729 36.318 1.000 25.89 ATOM 5074 O GLY C 202 99.636 47.319 35.753 1.000 32.59 ATOM 5075 N THR C 203 97.549 47.321 36.542 1.000 22.53 ATOM 5076 CA THR C 203 97.288 48.706 36.172 1.000 23.17 ATOM 5077 CB THR C 203 96.258 48.779 35.032 1.000 27.13 ATOM 5078 OD1 THR C 203 94.986 48.433 35.585 1.000 25.92 ATOM 5079 CG2 THR C 203 96.567 47.775 33.934 1.000 27.46 ATOM 5080 C THR C 203 96.769 49.464 37.391 1.000 29.62 ATOM 5081 O THR C 203 96.437 48.801 38.392 1.000 25.16 ATOM 5082 N PRO C 204 96.688 50.788 37.353 1.000 27.16 ATOM 5083 CD PRO C 204 97.155 51.684 36.277 1.000 27.74 ATOM 5084 CA PRO C 204 96.107 51.546 38.471 1.000 30.12 ATOM 5085 CE PRO C 204 96.141 52.996 37.970 1.000 28.02 ATOM 5086 CG PRO C 204 97.239 53.024 36.956 1.000 27.83 ATOM 5087 C PRO C 204 94.663 51.176 38.797 1.000 37.24 ATOM 5088 O PRO C 204 94.143 51.572 39.851 1.000 35.02 ATOM 5089 N LEU C 205 93.981 50.433 37.927 1.000 35.79 ATOM 5090 CA LEU C 205 92.608 50.024 38.223 1.000 30.70 ATOM 5091 CB LEU C 205 92.033 49.167 37.101 1.000 29.09 ATOM 5092 CG LEU C 205 90.536 48.854 37.159 1.000 35.68 ATOM 5093 CD1 LEU C 205 89.730 50.060 36.699 1.000 31.89 ATOM 5094 CD2 LEU C 205 90.211 47.615 36.337 1.000 31.92 ATOM 5095 C LEU C 205 92.579 49.247 39.538 1.000 30.14 ATOM 5096 O LEU C 205 91.648 49.387 40.329 1.000 36.81 ATOM 5097 N LEU C 206 93.605 48.425 39.734 1.000 31.90 ATOM 5098 CA LEU C 206 93.699 47.534 40.879 1.000 29.40 ATOM 5099 CE LEU C 206 94.474 46.273 40.479 1.000 25.89 ATOM 5100 CG LEU C 206 93.872 45.442 39.343 1.000 28.59 ATOM 5101 CD1 LEU C 206 94.364 43.998 39.404 1.000 29.19 ATOM 5102 CD2 LEU C 206 92.356 45.484 39.370 1.000 27.50 ATOM 5103 C LEU C 206 94.370 48.172 42.086 1.000 40.42 ATOM 5104 O LEU C 206 94.515 47.526 43.129 1.000 39.05 ATOM 5105 N THR C 207 94.798 49.431 41.989 1.000 42.35 ATOM 5106 CA THR C 207 95.542 50.010 43.106 1.000 48.45 ATOM 5107 CE THR C 207 96.139 51.382 42.745 1.000 49.14 ATOM 5108 OG1 THR C 207 97.202 51.198 41.798 1.000 62.11 ATOM 5109 CG2 THR C 207 96.756 52.042 43.969 1.000 47.12 ATOM 5110 C THR C 207 94.670 50.1534 4.352 1.000 52.40 ATOM 5111 O THR C 207 95.223 50.1784 5.452 1.000 44.87 ATOM 5112 N SER C 208 93.364 50.2404 4.157 1.000 57.38 ATOM 5113 CA SER C 208 92.357 50.4864 5.172 1.000 59.32 ATOM 5114 CE SER C 208 90.995 50.7944 4.529 1.000 59.37 ATOM 5115 OG SER C 208 91.092 51.8534 3.591 1.000 80.12 ATOM 5116 CB SER C 208 92.166 49.3194 6.133 1.000 61.87 ATOM 5117 O SER C 208 91.367 49.4084 7.070 1.000 69.52 ATOM 5118 N LEU C 209 92.876 48.2144 5.915 1.000 54.77 ATOM 5119 CA LEU C 209 92.625 47.0524 6.762 1.000 53.13 ATOM 5120 CE LEU C 209 92.245 45.838 45.916 1.000 53.90 ATOM 5121 CG LEU C 209 91.531 46.076 44.587 1.000 49.79 ATOM 5122 CD1 LEU C 209 92.130 45.191 43.502 1.000 35.07 ATOM 5123 CD2 LEU C 209 90.036 45.831 44.712 1.000 30.84 ATOM 5124 C LEU C 209 93.833 46.716 47.635 1.000 48.32 ATOM 5125 O LEU C 209 94.971 47.000 47.273 1.000 49.62 ATOM 5126 N PRO C 210 93.533 46.098 48.773 1.000 43.75 ATOM 5127 CD PRO C 210 92.167 45.769 49.215 1.000 47.38 ATOM 5128 CA PRO C 210 94.543 45.654 49.726 1.000 47.32 ATOM 5129 CB PRO C 210 93.764 44.736 50.672 1.000 44.91 ATOM 5130 CG PRO C 210 92.356 45.210 50.596 1.000 42.82 ATOM 5131 C PRO C 210 95.624 44.825 49.039 1.000 55.73 ATOM 5132 O PRO C 210 95.271 43.950 48.245 1.000 51.13 ATOM 5133 N GLU C 211 96.882 45.104 49.355 1.000 62.78 ATOM 5134 CA GLU C 211 97.985 44.332 48.782 1.000 65.71 ATOM 5135 CB GLU C 211 99.313 44.751 49.413 1.000 73.61 ATOM 5136 CG GLU C 211 100.508 43.921 48.979 1.000 78.96 ATOM 5137 CD GLU C 211 101.366 44.592 47.924 1.000 83.27 ATOM 5138 OE1 GLU C 211 100.804 45.229 47.007 1.000 78.56 ATOM 5139 OE2 GLU C 211 102.610 44.481 48.011 1.000 91.83 ATOM 5140 C GLU C 211 97.738 42.840 48.950 1.000 57.45 ATOM 5141 O GLU C 211 97.930 42.039 48.037 1.000 57.10 ATOM 5142 N LYS C 212 97.276 42.425 50.129 1.000 54.71 ATOM 5143 CA LYS C 212 96.958 41.008 50.289 1.000 53.11 ATOM 5144 CB LYS C 212 96.545 40.709 51.719 1.000 61.51 ATOM 5145 C LYS C 212 95.863 40.596 49.315 1.000 54.29 ATOM 5146 O LYS C 212 95.752 39.430 48.933 1.000 47.94 ATOM 5147 N VAL C 213 95.031 41.550 48.895 1.000 55.78 ATOM 5148 CA VAL C 213 93.969 41.196 47.948 1.000 59.39 ATOM 5149 CB VAL C 213 92.876 42.278 47.901 1.000 63.29 ATOM 5150 CG1 VAL C 213 91.983 42.096 46.683 1.000 59.66 ATOM 5151 CG2 VAL C 213 92.047 42.243 49.180 1.000 60.14 ATOM 5152 C VAL C 213 94.538 40.956 46.553 1.000 53.95 ATOM 5153 O VAL C 213 94.379 39.880 45.971 1.000 42.35 ATOM 5154 N ARG C 214 95.216 41.958 46.006 1.000 47.03 ATOM 5155 CA ARG C 214 95.901 41.833 44.729 1.000 45.10 ATOM 5156 CB ARG C 214 96.803 43.047 44.497 1.000 45.03 ATOM 5157 CG ARG C 214 96.359 43.982 43.393 1.000 50.46 ATOM 5158 CD ARG C 214 97.469 44.945 43.009 1.000 53.70 ATOM 5159 NE ARG C 214 98.264 45.387 44.148 1.000 52.31 ATOM 5160 CZ ARG C 214 97.821 46.112 45.165 1.000 49.37 ATOM 5161 NE1 ARG C 214 96.555 46.504 45.225 1.000 41.96 ATOM 5162 NH2 ARG C 214 98.657 46.447 46.139 1.000 51.95 ATOM 5163 C ARG C 214 96.753 40.570 44.668 1.000 38.21 ATOM 5164 O ARG C 214 96.561 39.721 43.803 1.000 46.16 ATOM 5165 N ASN C 215 97.704 40.460 45.592 1.000 39.14 ATOM 5166 CA ASN C 215 98.666 39.359 45.567 1.000 43.82 ATOM 5167 CE ASN C 215 99.623 39.443 46.757 1.000 42.67 ATOM 5168 CG ASN C 215 100.568 40.622 46.684 1.000 43.42 ATOM 5169 OD1 ASN C 215 101.050 40.994 45.614 1.000 54.29 ATOM 5170 ND2 ASN C 215 100.863 41.229 47.828 1.000 46.57 ATOM 5171 C ASN C 215 97.947 38.016 45.537 1.000 42.43 ATOM 5172 O ASN C 215 98.311 37.108 44.786 1.000 52.24 ATOM 5173 N PHE C 216 96.905 37.889 46.356 1.000 36.32 ATOM 5174 CA PHE C 216 96.124 36.660 46.348 1.000 33.94 ATOM 5175 CB PHE C 216 94.936 36.737 47.306 1.000 37.12 ATOM 5176 CG PHE C 216 94.029 35.518 47.179 1.000 43.40 ATOM 5177 CD1 PHE C 216 94.485 34.270 47.573 1.000 46.19 ATOM 5178 CD2 PHE C 216 92.751 35.642 46.668 1.000 44.18 ATOM 5179 CE1 PHE C 216 93.678 33.155 47.457 1.000 49.58 ATOM 5180 CE2 PHE C 216 91.937 34.532 46.553 1.000 46.42 ATOM 5181 CZ PHE C 216 92.400 33.288 46.943 1.000 48.68 ATOM 5182 C PHE C 216 95.622 36.362 44.932 1.000 36.62 ATOM 5183 O PHE C 216 95.951 35.308 44.393 1.000 35.34 ATOM 5184 N LEU C 217 94.855 37.295 44.383 1.000 38.86 ATOM 5185 CA LEU C 217 94.374 37.250 43.005 1.000 36.55 ATOM 5186 CB LEU C 217 93.819 38.603 42.563 1.000 41.84 ATOM 5187 CG LEU C 217 92.476 39.049 43.142 1.000 35.99 ATOM 5188 CD1 LEU C 217 92.146 40.475 42.727 1.000 34.52 ATOM 5189 CD2 LEU C 217 91.359 38.112 42.714 1.000 41.78 ATOM 5190 C LEU C 217 95.515 36.823 42.083 1.000 23.70 ATOM 5191 O LEU C 217 95.412 35.855 41.336 1.000 39.82 ATOM 5192 N ALA C 218 96.620 37.555 42.184 1.000 29.42 ATOM 5193 CA ALA C 218 97.825 37.237 41.433 1.000 33.94 ATOM 5194 CB ALA C 218 98.973 38.118 41.913 1.000 39.99 ATOM 5195 C ALA C 218 98.203 35.767 41.540 1.000 36.98 ATOM 5196 O ALA C 218 98.544 35.103 40.556 1.000 33.61 ATOM 5197 N SER C 219 98.161 35.216 42.751 1.000 33.61 ATOM 5198 CA SER C 219 98.612 33.844 42.946 1.000 33.83 ATOM 5199 CB SER C 219 98.711 33.556 44.453 1.000 37.13 ATOM 5200 OG SER C 219 97.402 33.337 44.963 1.000 40.94 ATOM 5201 C SER C 219 97.701 32.806 42.301 1.000 35.38 ATOM 5202 O SER C 219 98.063 31.628 42.222 1.000 28.50 ATOM 5203 N GLN C 220 96.522 33.218 41.845 1.000 33.22 ATOM 5204 CA GLN C 220 95.554 32.316 41.242 1.000 29.91 ATOM 5205 CE GLN C 220 94.138 32.880 41.421 1.000 35.00 ATOM 5206 CG GLN C 220 93.738 33.114 42.865 1.000 45.83 ATOM 5207 CD GLN C 220 93.228 31.841 43.519 1.000 55.68 ATOM 5208 OE1 GLN C 220 94.027 31.086 44.081 1.000 68.62 ATOM 5209 NE2 GLN C 220 91.922 31.615 43.432 1.000 59.51 ATOM 5210 C GLN C 220 95.780 32.064 39.754 1.000 26.22 ATOM 5211 O GLN C 220 95.211 31.112 39.214 1.000 25.79 ATOM 5212 N VAL C 221 96.581 32.877 39.073 1.000 23.25 ATOM 5213 CA VAL C 221 96.763 32.666 37.628 1.000 20.94 ATOM 5214 CB VAL C 221 97.491 33.870 37.009 1.000 21.52 ATOM 5215 CG1 VAL C 221 97.605 33.689 35.502 1.000 15.39 ATOM 5216 CG2 VAL C 221 96.782 35.168 37.379 1.000 17.44 ATOM 5217 C VAL C 221 97.548 31.396 37.375 1.000 25.25 ATOM 5218 O VAL C 221 98.681 31.277 37.853 1.000 26.36 ATOM 5219 N PRO C 222 96.990 30.413 36.682 1.000 26.70 ATOM 5220 CD PRO C 222 95.643 30.367 36.087 1.000 22.74 ATOM 5221 CA PRO C 222 97.725 29.149 36.494 1.000 24.77 ATOM 5222 CE PRO C 222 96.800 28.347 35.573 1.000 17.60 ATOM S223 CG PRO C 222 95.440 28.884 35.910 1.000 20.38 ATOM 5224 C PRO C 222 99.108 29.320 35.885 1.000 28.74 ATOM 5225 O PRO C 222 100.083 28.833 36.476 1.000 24.95 ATOM 5226 N PHE C 223 99.278 29.975 34.742 1.000 21.18 ATOM 5227 CA PHE C 223 100.619 30.161 34.198 1.000 17.83 ATOM 5228 CB PHE C 223 101.253 28.859 33.680 1.000 17.91 ATOM 5229 CG PHE C 223 102.659 29.160 33.145 1.000 27.36 ATOM 5230 CD1 PHE C 223 103.708 29.418 34.013 1.000 29.04 ATOM 5231 CD2 PHE C 223 102.917 29.189 31.788 1.000 23.22 ATOM 5232 CE1 PHE C 223 104.980 29.711 33.556 1.000 25.46 ATOM 5233 CE2 PHE C 223 104.179 29.483 31.314 1.000 23.84 ATOM 5234 CZ PHE C 223 105.216 29.750 32.189 1.000 25.17 ATOM 5235 C PHE C 223 100.609 31.174 33.058 1.000 27.06 ATOM 5236 O PHE C 223 99.820 31.006 32.117 1.000 27.00 ATOM 5237 N PRO C 224 101.451 32.202 33.097 1.000 27.86 ATOM 5238 CD PRO C 224 101.553 33.223 32.041 1.000 27.73 ATOM 5239 CA PRO C 224 102.399 32.439 34.187 1.000 29.28 ATOM 5240 CB PRO C 224 103.372 33.462 33.601 1.000 32.92 ATOM 5241 CG PRO C 224 102.618 34.157 32.523 1.000 29.32 ATOM 5242 C PRO C 224 101.716 33.013 35.425 1.000 27.75 ATOM 5243 O PRO C 224 100.771 33.787 35.301 1.000 23.30 ATOM 5244 N SER C 225 102.188 32.606 36.593 1.000 25.01 ATOM 5245 CA SER C 225 101.558 32.933 37.859 1.000 29.07 ATOM 5246 CB SER C 225 102.016 31.948 38.947 1.000 37.20 ATOM 5247 OG SER C 225 101.612 30.634 38.598 1.000 57.33 ATOM 5248 CB SER C 225 101.858 34.350 38.315 1.000 29.02 ATOM 5249 O SER C 225 102.663 34.588 39.219 1.000 31.13 ATOM 5250 N ARG C 226 101.192 35.299 37.675 1.000 22.75 ATOM 5251 CA ARG C 226 101.418 36.713 37.970 1.000 21.78 ATOM 5252 CB ARG C 226 102.787 37.164 37.456 1.000 21.27 ATOM 5253 CG ARG C 226 102.998 36.810 35.981 1.000 20.87 ATOM 5254 CD ARG C 226 103.943 37.804 35.323 1.000 23.93 ATOM 5255 NE ARG C 226 104.283 37.417 33.956 1.000 22.64 ATOM 5256 CZ ARG C 226 103.702 37.904 32.866 1.000 29.11 ATOM 5257 NH1 ARG C 226 104.094 37.476 31.668 1.000 20.68 ATOM 5258 NH2 ARG C 226 102.735 38.808 32.972 1.000 20.52 ATOM 5259 C ARG C 226 100.330 37.550 37.321 1.000 24.27 ATOM 5260 O ARG C 226 99.580 37.031 36.486 1.000 26.38 ATOM 5261 N LEU C 227 100.248 38.823 37.697 1.000 22.29 ATOM 5262 CA LEU C 227 99.365 39.717 36.947 1.000 25.06 ATOM 5263 CB LEU C 227 99.292 41.089 37.621 1.000 23.75 ATOM 5264 CG LEU C 227 98.844 41.076 39.092 1.000 23.95 ATOM 5265 CD1 LEU C 227 98.975 42.444 39.742 1.000 21.02 ATOM 5266 CD2 LEU C 227 97.414 40.579 39.194 1.000 19.70 ATOM 5267 C LEU C 227 99.875 39.829 35.514 1.000 26.87 ATOM 5268 O LEU C 227 101.080 39.746 35.238 1.000 20.04 ATOM 5269 N GLY C 228 98.964 40.039 34.562 1.000 24.87 ATOM 5270 CA GLY C 228 99.408 40.279 33.192 1.000 18.72 ATOM 5271 C GLY C 228 100.106 41.627 33.089 1.000 21.14 ATOM 5272 O GLY C 228 99.800 42.564 33.835 1.000 21.52 ATOM 5273 N ASP C 229 101.045 41.742 32.159 1.000 24.60 ATOM 5274 CA ASP C 229 101.741 43.004 31.910 1.000 21.43 ATOM 5275 CB ASP C 229 103.164 42.746 31.442 1.000 26.01 ATOM 5276 CG ASP C 229 104.006 44.001 31.340 1.000 37.41 ATOM 5277 OD1 ASP C 229 105.238 43.880 31.526 1.000 53.25 ATOM 5278 OD2 ASP C 229 103.477 45.102 31.082 1.000 38.34 ATOM 5279 C ASP C 229 100.973 43.799 30.860 1.000 19.57 ATOM 5280 O ASP C 229 100.660 43.204 29.824 1.000 23.49 ATOM 5281 N PRO C 230 100.661 45.059 31.112 1.000 22.69 ATOM 5282 CD PRO C 230 100.998 45.823 32.326 1.000 23.91 ATOM 5283 CA PRO C 230 99.893 45.861 30.152 1.000 21.64 ATOM 5284 CB PRO C 230 100.031 47.287 30.691 1.000 23.94 ATOM 5285 CG PRO C 230 100.194 47.090 32.168 1.000 24.54 ATOM 5286 C PRO C 230 100.469 45.765 28.744 1.000 25.45 ATOM 5287 O PRO C 230 99.706 45.781 27.779 1.000 25.01 ATOM 5288 N ALA C 231 101.789 45.633 28.634 1.000 24.95 ATOM 5289 CA ALA C 231 102.414 45.495 27.322 1.000 27.22 ATOM 5290 CB ALA C 231 103.933 45.490 27.425 1.000 23.00 ATOM 5291 C ALA C 231 101.924 44.231 26.614 1.000 25.34 ATOM 5292 O ALA C 231 101.917 44.192 25.385 1.000 27.31 ATOM 5293 N GLU C 232 101.523 43.222 27.375 1.000 23.62 ATOM 5294 CA GLU C 232 100.996 41.976 26.806 1.000 21.90 ATOM 5295 CB GLU C 232 100.999 40.864 27.853 1.000 21.70 ATOM 5296 CG GLU C 232 102.395 40.453 28.301 1.000 24.49 ATOM 5297 CD GLU C 232 102.451 39.569 29.525 1.000 22.86 ATOM 5298 OE1 GLU C 232 101.660 39.769 30.476 1.000 23.68 ATOM 5299 OE2 GLU C 232 103.296 38.648 29.576 1.000 22.83 ATOM 5300 C GLU C 232 99.607 42.219 26.227 1.000 20.51 ATOM 5301 O GLU C 232 99.202 41.633 25.226 1.000 21.77 ATOM 5302 N TYR C 233 98.841 43.115 26.856 1.000 20.18 ATOM 5303 CA TYR C 233 97.570 43.521 26.259 1.000 23.47 ATOM 5304 CB TYR C 233 96.766 44.393 27.226 1.000 20.77 ATOM 5305 CG TYR C 233 95.509 44.996 26.634 1.000 21.03 ATOM 5306 CD1 TYR C 233 94.302 44.305 26.635 1.000 19.12 ATOM 5307 CE1 TYR C 233 93.168 44.884 26.084 1.000 19.16 ATOM 5308 CD2 TYR C 233 95.521 46.266 26.069 1.000 17.67 ATOM 5309 CB2 TYR C 233 94.404 46.838 25.520 1.000 21.50 ATOM 5310 CZ TYR C 233 93.215 46.140 25.530 1.000 20.40 ATOM 5311 OH TYR C 233 92.105 46.738 24.972 1.000 20.20 ATOM 5312 C TYR C 233 97.856 44.254 24.947 1.000 26.17 ATOM 5313 O TYR C 233 97.257 44.012 23.905 1.000 24.88 ATOM 5314 N ALA C 234 98.775 45.210 24.983 1.000 23.28 ATOM 5315 CA ALA C 234 99.122 45.986 23.793 1.000 20.34 ATOM 5316 CE ALA C 234 100.225 46.981 24.114 1.000 25.63 ATOM 5317 C ALA C 234 99.527 45.064 22.646 1.000 20.70 ATOM 5318 O ALA C 234 99.126 45.278 21.502 1.000 22.04 ATOM 5319 N HIS C 235 100.323 44.045 22.979 1.000 21.74 ATOM 5320 CA HIS C 235 100.803 43.110 21.969 1.000 22.45 ATOM 5321 CE HIS C 235 101.734 42.052 22.566 1.000 20.97 ATOM 5322 CG HIS C 235 102.042 40.900 21.653 1.000 23.06 ATOM 5323 CD2 HIS C 235 101.439 39.716 21.406 1.000 20.44 ATOM 5324 ND1 HIS C 235 103.151 40.917 20.829 1.000 29.37 ATOM 5325 CB1 HIS C 235 103.200 39.803 20.128 1.000 24.08 ATOM 5326 NE2 HIS C 235 102.168 39.049 20.453 1.000 23.74 ATOM 5327 C HIS C 235 99.617 42.442 21.274 1.000 25.47 ATOM 5328 O HIS C 235 99.652 42.256 20.057 1.000 19.63 ATOM 5329 N LEU C 236 98.602 42.055 22.035 1.000 24.60 ATOM 5330 CA LEU C 236 97.441 41.381 21.445 1.000 22.50 ATOM 5331 CB LEU C 236 96.574 40.764 22.537 1.000 18.41 ATOM 5332 CG LEU C 236 95.340 39.987 22.079 1.000 21.33 ATOM 5333 CD1 LEU C 236 95.711 38.877 21.105 1.000 17.49 ATOM 5334 CD2 LEU C 236 94.587 39.408 23.281 1.000 15.39 ATOM 5335 C LEU C 236 96.631 42.339 20.576 1.000 22.47 ATOM 5336 O LEU C 236 96.032 41.921 19.585 1.000 21.32 ATOM 5337 N VAL C 237 96.603 43.614 20.927 1.000 21.37 ATOM 5338 CA VAL C 237 95.941 44.639 20.133 1.000 23.21 ATOM 5339 CB VAL C 237 96.008 46.029 20.800 1.000 24.40 ATOM 5340 CG1 VAL C 237 95.579 47.111 19.808 1.000 23.54 ATOM 5341 CG2 VAL C 237 95.158 46.088 22.064 1.000 21.30 ATOM 5342 C VAL C 237 96.587 44.742 18.750 1.000 27.11 ATOM 5343 O VAL C 237 95.920 44.818 17.718 1.000 20.91 ATOM 5344 N GLN C 238 97.920 44.767 18.730 1.000 23.43 ATOM 5345 CA GLN C 238 98.648 44.860 17.471 1.000 20.96 ATOM 5346 CB GLN C 238 100.156 44.994 17.711 1.000 25.92 ATOM 5347 CG GLN C 238 100.944 45.076 16.406 1.000 34.72 ATOM 5348 CD GLN C 238 102.331 45.670 16.621 1.000 45.75 ATOM 5349 CG1 GLN C 238 102.671 46.122 17.718 1.000 42.99 ATOM 5350 NE2 GLN C 238 103.139 45.672 15.565 1.000 37.12 ATOM 5351 C GLN C 238 98.406 43.631 16.610 1.000 17.47 ATOM 5352 O GLN C 238 98.163 43.729 15.409 1.000 31.42 ATOM 5353 N ALA C 239 98.471 42.462 17.226 1.000 13.40 ATOM 5354 CA ALA C 239 98.173 41.199 16.561 1.000 17.82 ATOM 5355 CB ALA C 239 98.167 40.051 17.556 1.000 20.85 ATOM 5356 C ALA C 239 96.831 41.264 15.840 1.000 23.82 ATOM 5357 O ALA C 239 96.671 40.812 14.702 1.000 22.62 ATOM 5358 N ILE C 240 95.851 41.848 16.538 1.000 21.62 ATOM 5359 CA ILE C 240 94.500 41.902 15.974 1.000 25.07 ATOM 5360 CE ILE C 240 93.479 42.245 17.069 1.000 24.15 ATOM 5361 CG2 ILE C 240 92.127 42.582 16.473 1.000 20.46 ATOM 5362 CD1 ILE C 240 93.340 41.152 18.139 1.000 17.17 ATOM 5363 CD1 ILE C 240 92.579 41.637 19.357 1.000 21.22 ATOM 5364 C ILE C 240 94.461 42.901 14.826 1.000 25.22 ATOM 5365 O ILE C 240 93.910 42.633 13.759 1.000 21.79 ATOM 5366 N ILE C 241 95.074 44.064 15.038 1.000 20.24 ATOM 5367 CA ILE C 241 95.171 45.059 13.974 1.000 25.86 ATOM 5368 CB ILE C 241 95.974 46.291 14.416 1.000 27.53 ATOM 5369 CG2 ILE C 241 96.380 47.147 13.218 1.000 24.99 ATOM 5370 CG1 ILE C 241 95.266 47.162 15.465 1.000 23.00 ATOM 5371 CD1 ILE C 241 96.201 48.192 16.082 1.000 20.65 ATOM 5372 C ILE C 241 95.810 44.445 12.731 1.000 27.42 ATOM 5373 O ILE C 241 95.363 44.672 11.603 1.000 25.67 ATOM 5374 N GLU C 242 96.864 43.656 12.910 1.000 21.24 ATOM 5375 CA GLU C 242 97.615 43.141 11.764 1.000 23.07 ATOM 5376 CE GLU C 242 98.992 42.649 12.234 1.000 21.75 ATOM 5377 CG GLU C 242 99.880 43.739 12.813 1.000 23.24 ATOM 5378 CD GLU C 242 101.247 43.211 13.211 1.000 32.86 ATOM 5379 OE1 GLU C 242 102.164 44.031 13.422 1.000 41.93 ATOM 5380 OE2 GLU C 242 101.415 41.976 13.324 1.000 38.32 ATOM 5381 C GLU C 242 96.896 42.024 11.021 1.000 27.62 ATOM 5382 O GLU C 242 97.032 41.898 9.796 1.000 25.36 ATOM 5383 N ASN C 243 96.135 41.200 11.737 1.000 20.54 ATOM 5384 CA ASN C 243 95.539 40.009 11.155 1.000 22.70 ATOM 5385 CE ASN C 243 95.428 38.910 12.223 1.000 20.67 ATOM 5386 CG ASN C 243 95.172 37.550 11.608 1.000 23.57 ATOM 5387 OD1 ASN C 243 94.183 37.346 10.889 1.000 21.00 ATOM 5388 ND2 ASN C 243 96.072 36.619 11.899 1.000 16.27 ATOM 5389 C ASN C 243 94.167 40.275 10.537 1.000 29.01 ATOM 5390 O ASN C 243 93.188 40.455 11.263 1.000 22.16 ATOM 5391 N PRO C 244 94.109 40.284 9.210 1.000 26.89 ATOM 5392 CD PRO C 244 95.226 39.922 8.304 1.000 24.01 ATOM 5393 CA PRO C 244 92.906 40.668 8.481 1.000 21.88 ATOM 5394 CB PRO C 244 93.357 40.639 7.003 1.000 24.45 ATOM 5395 CG PRO C 244 94.849 40.632 7.029 1.000 26.59 ATOM 5396 C PRO C 244 91.731 39.713 8.622 1.000 21.54 ATOM 5397 O PRO C 244 90.608 40.076 8.233 1.000 23.93 ATOM 5398 N PHE C 245 91.930 38.505 9.143 1.000 21.82 ATOM 5399 CA PHE C 245 90.804 37.570 9.215 1.000 19.75 ATOM 5400 CE PHE C 245 91.205 36.179 8.726 1.000 21.43 ATOM 5401 CG PHE C 245 90.140 35.467 7.909 1.000 19.34 ATOM 5402 CD1 PHE C 245 89.744 34.179 8.236 1.000 17.81 ATOM 5403 CD2 PHE C 245 89.551 36.074 6.816 1.000 18.35 ATOM 5404 CE1 PHE C 245 88.777 33.508 7.502 1.000 20.11 ATOM 5405 CE2 PHE C 245 88.574 35.423 6.080 1.000 16.76 ATOM 5406 CZ PHE C 245 88.181 34.145 6.416 1.000 17.96 ATOM 5407 C PHE C 245 90.221 37.480 10.620 1.000 24.50 ATOM 5408 O PHE C 245 89.310 36.688 10.858 1.000 20.21 ATOM 5409 N LEU C 246 90.718 38.285 11.553 1.000 24.14 ATOM 5410 CA LEU C 246 90.183 38.270 12.917 1.000 25.12 ATOM 5411 CB LEU C 246 91.275 38.644 13.922 1.000 21.84 ATOM 5412 CG LEU C 246 92.216 37.516 14.350 1.000 22.81 ATOM 5413 CD1 LEU C 246 93.366 38.063 15.192 1.000 22.23 ATOM 5414 CD2 LEU C 246 91.469 36.427 15.117 1.000 18.03 ATOM 5415 C LEU C 246 88.987 39.208 13.042 1.000 18.79 ATOM 5416 O LEU C 246 89.135 40.426 12.967 1.000 17.92 ATOM 5417 N ASN C 247 87.801 38.631 13.232 1.000 19.81 ATOM 5418 CA ASN C 247 86.606 39.468 13.280 1.000 22.54 ATOM 5419 CE ASN C 247 86.151 39.746 11.839 1.000 20.64 ATOM 5420 CG ASN C 247 85.230 40.938 11.705 1.000 27.10 ATOM 5421 OD1 ASN C 247 84.935 41.661 12.663 1.000 18.27 ATOM 5422 ND2 ASN C 247 84.767 41.143 10.468 1.000 23.10 ATOM 5423 C ASN C 247 85.473 38.824 14.070 1.000 17.99 ATOM 5424 O ASN C 247 85.265 37.616 14.005 1.000 16.75 ATOM 5425 N GLY C 248 84.724 39.640 14.801 1.000 19.04 ATOM 5426 CA GLY C 248 83.533 39.197 15.497 1.000 19.49 ATOM 5427 C GLY C 248 83.815 38.330 16.704 1.000 19.73 ATOM 5428 O GLY C 248 82.903 37.601 17.111 1.000 17.58 ATOM 5429 N GLU C 249 85.017 38.381 17.268 1.000 15.98 ATOM 5430 CA GLU C 249 85.389 37.405 18.302 1.000 16.41 ATOM 5431 CB GLU C 249 86.452 36.453 17.759 1.000 18.31 ATOM 5432 CG GLU C 249 87.296 35.682 18.759 1.000 19.50 ATOM 5433 CD GLU C 249 86.549 34.567 19.453 1.000 21.59 ATOM 5434 OE1 GLU C 249 87.127 33.491 19.715 1.000 24.29 ATOM 5435 OE2 GLU C 249 85.352 34.729 19.758 1.000 21.15 ATOM 5436 C GLU C 249 85.860 38.084 19.582 1.000 16.54 ATOM 5437 O GLU C 249 86.310 39.231 19.581 1.000 20.08 ATOM 5438 N VAL C 250 85.741 37.363 20.688 1.000 19.50 ATOM 5439 CA VAL C 250 86.236 37.744 22.003 1.000 14.75 ATOM 5440 CB VAL C 250 85.148 37.588 23.088 1.000 23.09 ATOM 5441 CD1 VAL C 250 85.708 37.916 24.463 1.000 20.21 ATOM 5442 CG2 VAL C 250 83.952 38.474 22.781 1.000 21.17 ATOM 5443 C VAL C 250 87.427 36.864 22.366 1.000 16.06 ATOM 5444 O VAL C 250 87.336 35.642 22.225 1.000 17.76 ATOM 5445 N ILE C 251 88.533 37.440 22.813 1.000 18.46 ATOM 5446 CA ILE C 251 89.715 36.640 23.141 1.000 19.52 ATOM 5447 CB ILE C 251 90.914 37.049 22.261 1.000 19.31 ATOM 5448 CG2 ILE C 251 92.214 36.427 22.753 1.000 17.15 ATOM 5449 CG1 ILE C 251 90.679 36.759 20.775 1.000 17.56 ATOM 5450 CD1 ILE C 251 91.777 37.281 19.878 1.000 19.77 ATOM 5451 C ILE C 251 90.104 36.808 24.602 1.000 17.13 ATOM 5452 O ILE C 251 90.381 37.941 25.018 1.000 20.67 ATOM 5453 N ARG C 252 90.135 35.707 25.349 1.000 17.57 ATOM 5454 CA ARG C 252 90.583 35.804 26.737 1.000 20.50 ATOM 5455 CB ARG C 252 90.206 34.567 27.548 1.000 20.54 ATOM 5456 CG ARG C 252 88.710 34.394 27.774 1.000 23.09 ATOM 5457 CD ARG C 252 88.441 33.054 28.452 1.000 21.26 ATOM 5458 NE ARG C 252 88.769 33.163 29.873 1.000 20.67 ATOM 5459 CZ ARG C 252 87.918 33.016 30.878 1.000 20.65 ATOM 5460 NE1 ARG C 252 88.351 33.143 32.127 1.000 16.60 ATOM 5461 NH2 ARG C 252 86.649 32.746 30.628 1.000 20.79 ATOM 5462 C ARG C 252 92.099 35.983 26.807 1.000 19.07 ATOM 5463 O ARG C 252 92.836 35.200 26.213 1.000 15.41 ATOM 5464 N LEU C 253 92.545 36.990 27.541 1.000 18.07 ATOM 5465 CA LEU C 253 93.977 37.197 27.787 1.000 17.32 ATOM 5466 CB LEU C 253 94.418 38.517 27.174 1.000 15.25 ATOM 5467 CG LEU C 253 95.903 38.874 27.253 1.000 21.28 ATOM 5468 CD1 LEU C 253 96.755 37.831 26.548 1.000 15.73 ATOM 5469 CD2 LEU C 253 96.176 40.255 26.668 1.000 15.80 ATOM 5470 C LEU C 253 94.202 37.152 29.293 1.000 20.34 ATOM 5471 O LEU C 253 94.062 38.178 29.959 1.000 18.61 ATOM 5472 N ASP C 254 94.497 35.971 29.835 1.000 18.39 ATOM 5473 CA ASP C 254 94.326 35.800 31.271 1.000 19.65 ATOM 5474 CB ASP C 254 92.830 35.489 31.527 1.000 16.16 ATOM 5475 CG ASP C 254 92.380 34.224 30.832 1.000 21.05 ATOM 5476 OD1 ASP C 254 93.218 33.505 30.235 1.000 19.41 ATOM 5477 OD2 ASP C 254 91.166 33.922 30.868 1.000 21.82 ATOM 5478 C ASP C 254 95.142 34.697 31.910 1.000 21.58 ATOM 5479 O ASP C 254 94.835 34.302 33.044 1.000 21.93 ATOM S480 N GLY C 255 96.168 34.157 31.255 1.000 19.98 ATOM 5481 CA GLY C 255 97.016 33.180 31.921 1.000 13.04 ATOM 5482 C GLY C 255 96.292 31.902 32.291 1.000 23.38 ATOM 5483 O GLY C 255 96.812 31.094 33.075 1.000 21.76 ATOM 5484 N ALA C 256 95.114 31.704 31.719 1.000 23.49 ATOM 5485 CA ALA C 256 94.304 30.505 31.855 1.000 20.27 ATOM 5486 CB ALA C 256 95.173 29.251 31.752 1.000 18.94 ATOM 5487 C ALA C 256 93.516 30.495 33.165 1.000 18.75 ATOM 5488 O ALA C 256 92.982 29.464 33.581 1.000 17.98 ATOM 5489 N ILE C 257 93.419 31.643 33.826 1.000 15.35 ATOM 5490 CA ILE C 257 92.646 31.696 35.059 1.000 21.12 ATOM 5491 CB ILE C 257 92.908 33.007 35.832 1.000 21.24 ATOM 5492 CG2 ILE C 257 92.148 34.173 35.216 1.000 23.06 ATOM 5493 CG1 ILE C 257 92.613 32.911 37.335 1.000 19.13 ATOM 5494 CD1 ILE C 257 92.930 34.191 38.084 1.000 19.06 ATOM 5495 C ILE C 257 91.155 31.560 34.783 1.000 25.65 ATOM 5496 O ILE C 257 90.677 31.973 33.729 1.000 19.69 ATOM 5497 N ARG C 258 90.438 30.984 35.738 1.000 24.39 ATOM 5498 CA ARG C 258 88.975 30.985 35.778 1.000 18.78 ATOM 5499 CB ARG C 258 88.376 29.617 35.523 1.000 17.15 ATOM 5500 CG ARG C 258 88.687 28.985 34.162 1.000 21.49 ATOM 5501 CD ARG C 258 88.076 29.820 33.052 1.000 23.58 ATOM 5502 NE ARG C 258 88.246 29.289 31.709 1.000 23.32 ATOM 5503 CZ ARG C 258 89.257 29.573 30.900 1.000 21.26 ATOM 5504 NE1 ARG C 258 89.306 29.031 29.691 1.000 17.94 ATOM 5505 NH2 ARG C 258 90.225 30.393 31.296 1.000 17.93 ATOM 5506 C ARG C 258 88.576 31.524 37.157 1.000 22.89 ATOM 5507 O ARG C 258 88.988 30.986 38.188 1.000 18.51 ATOM 5508 N MET C 259 87.810 32.604 37.219 1.000 22.41 ATOM 5509 CA MET C 259 87.600 33.245 38.516 1.000 22.89 ATOM 5510 CB MET C 259 87.145 34.696 38.321 1.000 23.35 ATOM 5511 CG MET C 259 88.029 35.503 37.385 1.000 27.42 ATOM 5512 SD MET C 259 89.757 35.470 37.881 1.000 26.67 ATOM 5513 CE MET C 259 89.731 36.436 39.387 1.000 27.72 ATOM 5514 C MET C 259 86.575 32.521 39.377 1.000 26.70 ATOM 5515 O MET C 259 85.478 32.178 38.947 1.000 25.54 ATOM 5516 N GLN C 260 86.946 32.305 40.631 1.000 30.71 ATOM 5517 CA GLN C 260 86.079 31.691 41.635 1.000 25.02 ATOM 5518 CB GLN C 260 86.967 30.983 42.653 1.000 27.72 ATOM 5519 CG GLN C 260 87.077 29.489 42.447 1.000 41.57 ATOM 5520 CD GLN C 260 86.158 28.897 41.402 1.000 49.91 ATOM 5521 OE1 GLN C 260 85.118 28.302 41.686 1.000 38.22 ATOM 5522 NE2 GLN C 260 86.536 29.040 40.134 1.000 67.27 ATOM 5523 C GLN C 260 85.182 32.743 42.277 1.000 25.92 ATOM 5524 O GLN C 260 85.403 33.942 42.054 1.000 24.17 ATOM 5525 N PRO C 261 84.165 32.365 43.041 1.000 23.99 ATOM 5526 CD PRO C 261 83.744 30.987 43.359 1.000 24.97 ATOM 5527 CA PRO C 261 83.289 33.372 43.662 1.000 22.83 ATOM 5528 CB PRO C 261 82.411 32.512 44.584 1.000 24.86 ATOM 5529 CG PRO C 261 82.334 31.209 43.849 1.000 25.45 ATOM 5530 C PRO C 261 84.067 34.409 44.457 1.000 22.13 ATOM 5531 OT1 PRO C 261 85.046 33.998 45.112 1.000 24.75 ATOM 5532 OT2 PRO C 261 83.742 35.620 44.416 1.000 17.73 ATOM 5533 PN LIG C 262 92.798 49.871 33.096 1.000 25.36 ATOM 5534 O1N LIG C 262 93.331 48.582 33.757 1.000 23.33 ATOM 5535 O2N LIG C 262 93.836 50.420 32.122 1.000 22.34 ATOM 5536 O3P LIG C 262 92.507 50.871 34.244 1.000 30.26 ATOM 5537 O5M LIG C 262 91.425 49.583 32.332 1.000 24.41 ATOM 5538 C5M LIG C 262 91.307 49.563 30.881 1.000 31.36 ATOM 5539 C4M LIG C 262 90.121 48.645 30.417 1.000 32.73 ATOM 5540 O4M LIG C 262 90.448 47.263 30.689 1.000 32.21 ATOM 5541 C3M LIG C 262 88.788 48.924 31.157 1.000 30.15 ATOM 5542 O3M LIG C 262 87.691 48.676 30.252 1.000 18.36 ATOM 5543 C2M LIG C 262 88.844 47.876 32.303 1.000 22.20 ATOM 5544 O2M LIG C 262 87.499 47.638 32.766 1.000 20.27 ATOM 5545 C1M LIG C 262 89.414 46.665 31.519 1.000 26.13 ATOM 5546 N1N LIG C 262 89.909 45.522 32.334 1.000 20.70 ATOM 5547 C6N LIG C 262 89.174 44.261 32.234 1.000 15.32 ATOM 5548 C5N LIG C 262 89.567 43.176 32.919 1.000 17.17 ATOM 5549 C4N LIG C 262 90.602 43.316 34.065 1.000 24.88 ATOM 5550 C3N LIG C 262 91.525 44.563 33.874 1.000 22.18 ATOM 5551 C2N LIG C 262 91.080 45.645 33.211 1.000 20.26 ATOM 5552 C7N LIG C 262 92.742 44.623 34.786 1.000 15.83 ATOM 5553 O7N LIG C 262 93.089 43.625 35.432 1.000 23.87 ATOM 5554 N7N LIG C 262 93.389 45.767 34.842 1.000 19.65 ATOM 5555 PA LIG C 262 92.957 52.330 34.413 1.000 25.29 ATOM 5556 O1A LIG C 262 92.097 52.960 35.526 1.000 22.89 ATOM 5557 O2A LIG C 262 94.442 52.459 34.747 1.000 23.14 ATOM 5558 O5B LIG C 262 92.661 53.176 33.089 1.000 24.87 ATOM 5559 C5B LIG C 262 91.287 53.396 32.644 1.000 23.91 ATOM 5560 C4B LIG C 262 91.188 54.791 31.966 1.000 22.53 ATOM 5561 O4B LIG C 262 89.830 55.059 31.517 1.000 24.50 ATOM 5562 C3B LIG C 262 91.629 55.950 32.901 1.000 25.27 ATOM 5563 O3B LIG C 262 92.747 56.674 32.359 1.000 23.62 ATOM 5564 C2B LIG C 262 90.370 56.828 32.945 1.000 24.04 ATOM 5565 O2B LIG C 262 90.615 58.207 33.212 1.000 22.80 ATOM 5566 C1B LIG C 262 89.689 56.509 31.591 1.000 25.73 ATOM 5567 N9A LIG C 262 88.235 56.865 31.670 1.000 25.45 ATOM 5568 C4A LIG C 262 87.449 57.586 30.775 1.000 27.43 ATOM 5569 N3A LIG C 262 87.701 58.238 29.493 1.000 22.57 ATOM 5570 C2A LIG C 262 86.659 58.824 28.955 1.000 29.08 ATOM 5571 N1A LIG C 262 85.421 58.916 29.403 1.000 34.71 ATOM 5572 C6A LIG C 262 85.094 58.361 30.556 1.000 25.70 ATOM 5573 C5A LIG C 262 86.096 57.654 31.327 1.000 25.70 ATOM 5574 N7A LIG C 262 86.008 56.994 32.545 1.000 27.04 ATOM 5575 C8A LIG C 262 87.303 56.572 32.659 1.000 22.87 ATOM 5576 N6A LIG C 262 83.874 58.533 31.055 1.000 21.84 ATOM 5577 C LIG C 262 87.768 44.396 41.110 1.000 44.98 ATOM 5578 C1 LIG C 262 86.511 43.552 41.617 1.000 48.30 ATOM 5579 N LIG C 262 86.430 43.126 42.940 1.000 48.50 ATOM 5580 O LIG C 262 85.605 43.293 40.797 1.000 65.58 ATOM 5581 C2 LIG C 262 87.563 43.453 43.877 1.000 51.16 ATOM 5582 C3 LIG C 262 88.661 42.332 43.896 1.000 52.13 ATOM 5583 C4 LIG C 262 85.251 42.324 43.394 1.000 42.63 ATOM 5584 CB LIG C 262 85.547 40.804 43.209 1.000 53.20 ATOM 5585 C6 LIG C 262 86.952 40.386 43.681 1.000 61.97 ATOM 5586 C7 LIG C 262 88.182 41.098 43.084 1.000 58.52 ATOM 5587 C8 LIG C 262 87.768 45.903 41.567 1.000 36.21 ATOM 5588 C9 LIG C 262 89.004 46.569 41.608 1.000 38.49 ATOM 5589 C10 LIG C 262 89.074 47.902 41.999 1.000 36.24 ATOM 5590 C11 LIG C 262 87.912 48.581 42.357 1.000 39.07 ATOM 5591 C12 LIG C 262 86.681 47.933 42.332 1.000 39.17 ATOM 5592 C13 LIG C 262 86.610 46.607 41.906 1.000 37.44 ATOM 5593 C15 LIG C 262 87.326 45.081 38.785 1.000 36.27 ATOM 5594 N1 LIG C 262 87.409 45.213 37.494 1.000 33.45 ATOM 5595 C16 LIG C 262 88.460 44.477 36.824 1.000 31.46 ATOM 5596 C17 LIG C 262 89.357 43.657 37.546 1.000 38.18 ATOM 5597 C18 LIG C 262 89.189 43.536 39.079 1.000 40.16 ATOM 5598 N2 LIG C 262 88.040 44.343 39.596 1.000 42.60 ATOM 5599 S LIG C 262 90.274 42.506 40.037 1.000 37.80 ATOM 5600 C19 LIG C 262 90.242 43.067 36.680 1.000 36.22 ATOM 5601 N3 LIG C 262 89.906 43.510 35.401 1.000 27.95 ATOM 5602 N4 LIG C 262 88.875 44.403 35.1515 1.000 28.88 ATOM 5603 CB SER D 7 53.786 21.308 43.599 1.000 44.31 ATOM 5604 CB SER D 7 55.174 23.307 43.111 1.000 42.72 ATOM 5605 O SER D 7 55.885 23.720 44.027 1.000 47.89 ATOM 5606 N SER D 7 56.230 21.111 43.360 1.000 57.68 ATOM 5607 CA SER D 7 55.040 21.806 42.892 1.000 49.63 ATOM 5608 N VAL D 8 54.494 24.107 42.293 1.000 38.26 ATOM 5609 CA VAL D 8 54.523 25.551 42.518 1.000 36.32 ATOM 5610 CB VAL D 8 54.535 26.343 41.198 1.000 39.50 ATOM 5611 CD1 VAL D 8 55.802 26.044 40.408 1.000 35.22 ATOM 5612 CG2 VAL D 8 53.297 26.026 40.374 1.000 29.19 ATOM 5613 C VAL D 8 53.322 25.979 43.354 1.000 30.87 ATOM 5614 O VAL D 8 53.141 27.156 43.662 1.000 32.37 ATOM 5615 N LYS D 9 52.480 25.013 43.716 1.000 26.77 ATOM 5616 CA LYS D 9 51.272 25.363 44.468 1.000 29.29 ATOM 5617 CB LYS D 9 50.441 24.118 44.724 1.000 28.07 ATOM 5618 C LYS D 9 51.638 26.078 45.761 1.000 31.62 ATOM 5619 O LYS D 9 52.452 25.599 46.552 1.000 32.26 ATOM 5620 N GLY D 10 51.051 27.248 45.989 1.000 34.81 ATOM 5621 CA GLY D 10 51.322 28.015 47.187 1.000 30.81 ATOM 5622 C GLY D 10 52.453 29.007 47.078 1.000 33.23 ATOM 5623 O GLY D 10 52.595 29.858 47.972 1.000 38.22 ATOM 5624 N LEU D 11 53.281 28.950 46.032 1.000 29.06 ATOM 5625 CA LEU D 11 54.341 29.952 45.907 1.000 27.91 ATOM 5626 CB LEU D 11 55.443 29.526 44.933 1.000 26.09 ATOM 5627 CG LEU D 11 56.089 28.165 45.194 1.000 33.28 ATOM 5628 CD1 LEU D 11 57.196 27.900 44.183 1.000 37.73 ATOM 5629 CD2 LEU D 11 56.621 28.095 46.615 1.000 29.82 ATOM 5630 C LEU D 11 53.763 31.284 45.430 1.000 24.63 ATOM 5631 O LEU D 11 52.771 31.295 44.706 1.000 23.43 ATOM 5632 N VAL D 12 54.404 32.369 45.829 1.000 21.94 ATOM 5633 CA VAL D 12 54.083 33.706 45.366 1.000 23.89 ATOM 5634 CB VAL D 12 53.982 34.683 46.548 1.000 26.77 ATOM 5635 CG1 VAL D 12 53.686 36.091 46.052 1.000 23.82 ATOM 5636 CG2 VAL D 12 52.918 34.211 47.534 1.000 26.90 ATOM 5637 C VAL D 12 55.133 34.211 44.377 1.000 29.60 ATOM 5638 O VAL D 12 56.302 34.357 44.727 1.000 26.47 ATOM 5639 N ALA D 13 54.713 34.480 43.144 1.000 29.25 ATOM 5640 CA ALA D 13 55.601 34.896 42.073 1.000 23.99 ATOM 5641 CB ALA D 13 55.430 33.937 40.899 1.000 23.74 ATOM 5642 C ALA D 13 55.353 36.314 41.589 1.000 25.67 ATOM 5643 O ALA D 13 54.228 36.704 41.266 1.000 30.62 ATOM 5644 N VAL D 14 56.414 37.106 41.512 1.000 19.86 ATOM 5645 CA VAL D 14 56.311 38.445 40.929 1.000 21.74 ATOM 5646 CB VAL D 14 57.112 39.480 41.716 1.000 24.02 ATOM 5647 CD1 VAL D 14 57.244 40.807 40.988 1.000 22.87 ATOM 5648 CG2 VAL D 14 56.442 39.698 43.074 1.000 26.38 ATOM 5649 C VAL D 14 56.791 38.337 39.483 1.000 28.01 ATOM 5650 O VAL D 14 57.918 37.883 39.272 1.000 27.09 ATOM 5651 N ILE D 15 55.940 38.706 38.537 1.000 23.88 ATOM 5652 CA ILE D 15 56.238 38.541 37.107 1.000 22.25 ATOM 5653 CB ILE D 15 55.209 37.576 36.480 1.000 24.05 ATOM 5654 CG2 ILE D 15 55.384 37.441 34.975 1.000 24.05 ATOM 5655 CD1 ILE D 15 55.217 36.202 37.157 1.000 25.78 ATOM 5656 CD1 ILE D 15 54.092 35.286 36.735 1.000 27.73 ATOM 5657 C ILE D 15 56.236 39.867 36.377 1.000 23.91 ATOM 5658 O ILE D 15 55.197 40.468 36.084 1.000 22.19 ATOM 5659 N THR D 16 57.422 40.381 36.057 1.000 22.27 ATOM 5660 CA THR D 16 57.473 41.647 35.332 1.000 21.40 ATOM 5661 CB THR D 16 58.852 42.310 35.441 1.000 22.25 ATOM 5662 OD1 THR D 16 59.739 41.705 34.490 1.000 20.62 ATOM 5663 CG2 THR D 16 59.449 42.046 36.817 1.000 18.29 ATOM 5664 C THR D 16 57.118 41.385 33.869 1.000 20.63 ATOM 5665 O THR D 16 57.369 40.282 33.371 1.000 22.61 ATOM 5666 N GLY D 17 56.532 42.383 33.216 1.000 21.88 ATOM 5667 CA GLY D 17 56.018 42.192 31.864 1.000 23.48 ATOM 5668 C GLY D 17 54.858 41.203 31.908 1.000 26.78 ATOM 5669 O GLY D 17 54.552 40.526 30.929 1.000 21.03 ATOM 5670 N GLY D 18 54.204 41.113 33.073 1.000 24.25 ATOM 5671 CA GLY D 18 53.134 40.161 33.270 1.000 20.46 ATOM 5672 C GLY D 18 51.874 40.412 32.475 1.000 23.10 ATOM 5673 O GLY D 18 51.018 39.524 32.358 1.000 23.13 ATOM 5674 N ALA D 19 51.687 41.600 31.895 1.000 23.45 ATOM 5675 CA ALA D 19 50.447 41.865 31.168 1.000 23.54 ATOM 5676 CB ALA D 19 50.253 43.372 31.030 1.000 20.54 ATOM 5677 C ALA D 19 50.413 41.221 29.793 1.000 30.19 ATOM 5678 O ALA D 19 49.368 41.176 29.136 1.000 31.79 ATOM 5679 N SER D 20 51.542 40.719 29.294 1.000 26.00 ATOM 5680 CA SER D 20 51.553 40.290 27.891 1.000 25.37 ATOM 5681 CB SER D 20 51.882 41.515 27.031 1.000 27.24 ATOM 5682 OG SER D 20 52.044 41.220 25.656 1.000 28.53 ATOM 5683 C SER D 20 52.538 39.156 27.637 1.000 29.51 ATOM 5684 O SER D 20 53.405 38.868 28.468 1.000 26.87 ATOM 5685 N GLY D 21 52.401 38.522 26.478 1.000 26.73 ATOM 5686 CA GLY D 21 53.282 37.503 25.962 1.000 23.45 ATOM 5687 C GLY D 21 53.811 36.496 26.953 1.000 27.95 ATOM 5688 O GLY D 21 53.075 35.789 27.642 1.000 22.21 ATOM 5689 N LEU D 22 55.138 36.386 27.043 1.000 23.99 ATOM 5690 CA LEU D 22 55.762 35.360 27.868 1.000 20.60 ATOM 5691 CB LEU D 22 57.284 35.376 27.669 1.000 21.35 ATOM 5692 CG LEU D 22 57.781 35.299 26.219 1.000 20.42 ATOM 5693 CD1 LEU D 22 59.304 35.218 26.169 1.000 17.83 ATOM 5694 CD2 LEU D 22 57.149 34.113 25.507 1.000 17.30 ATOM 5695 C LEU D 22 55.418 35.543 29.342 1.000 18.64 ATOM 5696 O LEU D 22 55.110 34.564 30.024 1.000 23.17 ATOM 5697 N GLY D 23 55.470 36.772 29.837 1.000 20.39 ATOM 5698 CA GLY D 23 55.160 37.003 31.250 1.000 26.89 ATOM 5699 C GLY D 23 53.729 36.587 31.565 1.000 28.07 ATOM 5700 O GLY D 23 53.461 35.908 32.559 1.000 23.44 ATOM 5701 N LEU D 24 52.798 36.985 30.692 1.000 20.84 ATOM 5702 CA LEU D 24 51.399 36.626 30.897 1.000 20.18 ATOM 5703 CB LEU D 24 50.506 37.238 29.813 1.000 20.69 ATOM 5704 CG LEU D 24 49.044 36.782 29.835 1.000 23.66 ATOM 5705 CD1 LEU D 24 48.396 37.166 31.159 1.000 22.35 ATOM 5706 CD2 LEU D 24 48.263 37.369 28.667 1.000 23.89 ATOM 5707 C LEU D 24 51.211 35.116 30.911 1.000 23.44 ATOM 5708 O LEU D 24 50.522 34.570 31.770 1.000 23.82 ATOM 5709 N ALA D 25 51.827 34.444 29.936 1.000 25.43 ATOM 5710 CA ALA D 25 51.716 32.995 29.824 1.000 20.00 ATOM 5711 CB ALA D 25 52.417 32.500 28.560 1.000 22.34 ATOM 5712 C ALA D 25 52.290 32.296 31.049 1.000 24.36 ATOM 5713 O ALA D 25 51.801 31.264 31.514 1.000 26.51 ATOM 5714 N THR D 26 53.360 32.880 31.582 1.000 24.33 ATOM 5715 CA THR D 26 53.939 32.353 32.816 1.000 22.92 ATOM 5716 CB THR D 26 55.245 33.096 33.133 1.000 25.10 ATOM 5717 OG1 THR D 26 56.140 32.896 32.023 1.000 22.29 ATOM 5718 CG2 THR D 26 55.950 32.532 34.356 1.000 18.54 ATOM 5719 C THR D 26 52.926 32.461 33.948 1.000 21.41 ATOM 5720 O THR D 26 52.680 31.516 34.693 1.000 25.68 ATOM 5721 N ALA D 27 52.308 33.630 34.070 1.000 21.76 ATOM 5722 CA ALA D 27 51.305 33.847 35.110 1.000 25.16 ATOM 5723 CB ALA D 27 50.825 35.288 35.048 1.000 26.09 ATOM 5724 C ALA D 27 50.158 32.863 34.969 1.000 27.42 ATOM 5725 O ALA D 27 49.716 32.221 35.925 1.000 23.96 ATOM 5726 N GLU D 28 49.668 32.736 33.740 1.000 23.93 ATOM 5727 CA GLU D 28 48.597 31.791 33.452 1.000 26.72 ATOM 5728 CB GLU D 28 48.315 31.748 31.938 1.000 24.65 ATOM 5729 CG GLU D 28 47.483 32.934 31.478 1.000 29.35 ATOM 5730 CD GLU D 28 47.321 33.034 29.978 1.000 36.70 ATOM 5731 OE1 GLU D 28 46.571 33.939 29.548 1.000 40.71 ATOM 5732 OE2 GLU D 28 47.928 32.235 29.233 1.000 41.27 ATOM 5733 C GLU D 28 48.941 30.392 33.936 1.000 29.67 ATOM 5734 O GLU D 28 48.133 29.698 34.550 1.000 23.91 ATOM 5735 N ARG D 29 50.172 29.962 33.633 1.000 26.23 ATOM 5736 CA ARG D 29 50.523 28.585 33.958 1.000 23.90 ATOM 5737 CB ARG D 29 51.803 28.148 33.242 1.000 23.31 ATOM 5738 CG ARG D 29 52.083 26.668 33.457 1.000 25.31 ATOM 5739 CD ARG D 29 53.346 26.249 32.723 1.000 26.40 ATOM 5740 NE ARG D 29 53.683 24.857 33.006 1.000 26.23 ATOM 5741 CZ ARG D 29 53.139 23.821 32.384 1.000 30.28 ATOM 5742 NE1 ARG D 29 53.514 22.595 32.717 1.000 31.68 ATOM 5743 NH2 ARG D 29 52.228 23.996 31.437 1.000 28.63 ATOM 5744 C ARG D 29 50.683 28.409 35.458 1.000 28.09 ATOM 5745 O ARG D 29 50.170 27.451 36.043 1.000 34.40 ATOM 5746 N LEU D 30 51.387 29.336 36.106 1.000 23.92 ATOM 5747 CA LEU 0 30 51.611 29.157 37.541 1.000 25.83 ATOM 5748 CE LEU D 30 52.632 30.169 38.042 1.000 28.15 ATOM 5749 CG LEU D 30 54.051 30.067 37.460 1.000 26.33 ATOM 5750 CD1 LEU D 30 54.925 31.168 38.048 1.000 18.28 ATOM 5751 CD2 LEU D 30 54.641 28.690 37.714 1.000 25.83 ATOM 5752 C LEU D 30 50.301 29.263 38.310 1.000 32.25 ATOM 5753 O LEU D 30 50.025 28.452 39.205 1.000 32.13 ATOM 5754 N VAL D 31 49.483 30.260 37.968 1.000 28.07 ATOM 5755 CA VAL D 31 48.206 30.370 38.681 1.000 30.63 ATOM 5756 CB VAL D 31 47.387 31.593 38.255 1.000 33.71 ATOM 5757 CD1 VAL D 31 45.995 31.535 38.883 1.000 43.21 ATOM 5758 CG2 VAL D 31 48.069 32.889 38.652 1.000 28.34 ATOM 5759 C VAL D 31 47.410 29.084 38.467 1.000 33.51 ATOM 5760 O VAL D 31 46.844 28.504 39.398 1.000 34.58 ATOM 5761 N GLY D 32 47.411 28.612 37.220 1.000 27.31 ATOM 5762 CA GLY D 32 46.738 27.367 36.888 1.000 26.97 ATOM 5763 C GLY D 32 47.258 26.226 37.749 1.000 36.82 ATOM 5764 O GLY D 32 46.510 25.290 38.045 1.000 33.72 ATOM 5765 N GLN D 33 48.523 26.305 38.162 1.000 34.44 ATOM 5766 CA GLN D 33 49.118 25.225 38.942 1.000 36.67 ATOM 5767 CB GLN D 33 50.598 25.042 38.600 1.000 40.13 ATOM 5768 CG GLN D 33 50.936 24.989 37.130 1.000 44.78 ATOM 5769 CD GLN D 33 50.949 23.598 36.543 1.000 49.17 ATOM 5770 OE1 GLN D 33 50.361 22.654 37.070 1.000 57.52 ATOM 5771 NE2 GLN D 33 51.641 23.474 35.415 1.000 56.34 ATOM 5772 C GLN D 33 48.992 25.447 40.449 1.000 34.31 ATOM 5773 O GLN D 33 49.590 24.700 41.232 1.000 32.93 ATOM 5774 N GLY D 34 48.233 26.456 40.867 1.000 33.15 ATOM 5775 CA GLY D 34 48.047 26.729 42.280 1.000 29.31 ATOM 5776 C GLY D 34 48.915 27.821 42.841 1.000 32.67 ATOM 5777 O GLY D 34 48.846 28.101 44.047 1.000 33.83 ATOM 5778 N ALA D 35 49.757 28.501 42.055 1.000 26.73 ATOM 5779 CA ALA D 35 50.585 29.543 42.668 1.000 22.64 ATOM 5780 CB ALA D 35 51.868 29.730 41.868 1.000 25.14 ATOM 5781 C ALA D 35 49.853 30.869 42.767 1.000 22.80 ATOM 5782 O ALA D 35 48.780 31.033 42.187 1.000 27.59 ATOM 5783 N SER D 36 50.425 31.840 43.480 1.000 24.27 ATOM 5784 CA SER D 36 49.868 33.188 43.417 1.000 29.41 ATOM 5785 CE SER D 36 49.675 33.820 44.794 1.000 28.13 ATOM 5786 OG SER D 36 48.888 33.000 45.629 1.000 35.10 ATOM 5787 CB SER D 36 50.780 34.070 42.566 1.000 34.62 ATOM 5788 O SER D 36 52.001 33.922 42.600 1.000 26.36 ATOM 5789 N ALA D 37 50.183 34.989 41.804 1.000 30.49 ATOM 5790 CA ALA D 37 51.027 35.871 41.007 1.000 29.17 ATOM 5791 CB ALA D 37 50.974 35.474 39.531 1.000 29.10 ATOM 5792 C ALA D 37 50.639 37.334 41.162 1.000 24.61 ATOM 5793 O ALA D 37 49.474 37.691 41.294 1.000 29.85 ATOM 5794 N VAL D 38 51.665 38.171 41.122 1.000 23.25 ATOM 5795 CA VAL D 38 51.557 39.605 40.983 1.000 22.55 ATOM 5796 CB VAL D 38 52.353 40.353 42.059 1.000 26.24 ATOM 5797 CG1 VAL D 38 52.402 41.841 41.739 1.000 25.94 ATOM 5798 CG2 VAL D 38 51.759 40.097 43.435 1.000 30.97 ATOM 5799 C VAL D 38 52.098 40.009 39.606 1.000 29.14 ATOM 5800 O VAL D 38 53.286 39.804 39.349 1.000 22.57 ATOM 5801 N LEU D 39 51.233 40.554 38.765 1.000 27.12 ATOM 5802 CA LEU D 39 51.591 41.039 37.446 1.000 24.31 ATOM 5803 CE LEU D 39 50.407 41.028 36.480 1.000 23.52 ATOM 5804 CD LEU D 39 49.520 39.788 36.443 1.000 22.65 ATOM 5805 CD1 LEU D 39 48.490 39.894 35.319 1.000 23.91 ATOM 5806 CD2 LEU D 39 50.323 38.512 36.274 1.000 20.23 ATOM 5807 C LEU D 39 52.135 42.463 37.552 1.000 26.76 ATOM 5808 O LEU D 39 51.395 43.411 37.806 1.000 27.20 ATOM 5809 N LEU D 40 53.446 42.591 37.357 1.000 24.31 ATOM 5810 CA LEU D 40 54.093 43.898 37.390 1.000 21.37 ATOM 5811 CB LEU D 40 55.397 43.828 38.163 1.000 17.64 ATOM 5812 CG LEU D 40 56.086 45.095 38.628 1.000 25.08 ATOM 5813 CD1 LEU D 40 57.124 44.741 39.693 1.000 28.62 ATOM 5814 CD2 LEU D 40 56.791 45.854 37.505 1.000 26.98 ATOM 5815 C LEU D 40 54.300 44.376 35.954 1.000 27.49 ATOM 5816 O LEU D 40 55.085 43.804 35.204 1.000 25.14 ATOM 5817 N ASP D 41 53.609 45.447 35.588 1.000 30.57 ATOM 5818 CA ASP D 41 53.638 45.950 34.221 1.000 26.01 ATOM 5819 CB ASP D 41 52.768 45.058 33.334 1.000 20.45 ATOM 5820 CG ASP D 41 53.280 45.012 31.903 1.000 26.61 ATOM 5821 OD1 ASP D 41 53.563 46.116 31.385 1.000 25.97 ATOM 5822 OD2 ASP D 41 53.385 43.906 31.331 1.000 23.68 ATOM 5823 C ASP D 41 53.181 47.404 34.179 1.000 29.66 ATOM 5824 O ASP D 41 52.708 47.942 35.186 1.000 24.67 ATOM 5825 N LEU D 42 53.341 48.039 33.022 1.000 26.33 ATOM 5826 CA LEU D 42 53.102 49.477 32.902 1.000 28.41 ATOM 5827 CE LEU D 42 53.603 49.989 31.549 1.000 26.22 ATOM 5828 CD LEU D 42 55.111 49.853 31.294 1.000 29.25 ATOM 5829 CD1 LEU D 42 55.433 50.075 29.825 1.000 25.00 ATOM 5830 CD2 LEU D 42 55.908 50.811 32.166 1.000 18.73 ATOM 5831 C LEU D 42 51.623 49.797 33.102 1.000 25.26 ATOM 5832 O LEU D 42 50.789 48.919 32.898 1.000 19.04 ATOM 5833 N PRO D 43 51.318 51.028 33.489 1.000 30.00 ATOM 5834 CD PRO D 43 52.263 52.138 33.658 1.000 29.98 ATOM 5835 CA PRO D 43 49.934 51.405 33.789 1.000 31.92 ATOM 5836 CE PRO D 43 50.025 52.856 34.254 1.000 27.79 ATOM 5837 CG PRO D 43 51.444 53.272 34.182 1.000 33.26 ATOM 5838 C PRO D 43 49.022 51.329 32.565 1.000 31.69 ATOM 5839 O PRO D 43 47.857 50.955 32.686 1.000 32.45 ATOM 5840 N ASN D 44 49.559 51.699 31.407 1.000 29.00 ATOM 5841 CA ASN D 44 48.730 51.669 30.199 1.000 39.63 ATOM 5842 CB ASN D 44 49.250 52.700 29.196 1.000 46.89 ATOM 5843 CG ASN D 44 50.723 52.510 28.894 1.000 51.07 ATOM 5844 OD1 ASN D 44 51.612 53.038 29.546 1.000 67.13 ATOM 5845 ND2 ASN D 44 50.973 51.715 27.861 1.000 61.81 ATOM 5846 C ASN D 44 48.686 50.276 29.595 1.000 36.13 ATOM 5847 O ASN D 44 48.082 50.038 28.548 1.000 38.91 ATOM 5848 N SER D 45 49.338 49.310 30.242 1.000 32.04 ATOM 5849 CA SER D 45 49.150 47.933 29.771 1.000 32.95 ATOM 5850 CE SER D 45 50.283 47.018 30.216 1.000 32.23 ATOM 5851 OG SER D 45 50.313 46.891 31.627 1.000 27.59 ATOM 5852 CB SER D 45 47.794 47.444 30.273 1.000 35.99 ATOM 5853 O SER D 45 47.174 48.092 31.123 1.000 65.28 ATOM 5854 N GLY D 46 47.305 46.319 29.762 1.000 33.63 ATOM 5855 CA GLY D 46 46.034 45.794 30.260 1.000 32.91 ATOM 5856 C GLY D 46 46.236 44.777 31.371 1.000 30.01 ATOM 5857 O GLY D 46 45.515 43.789 31.487 1.000 32.99 ATOM 5858 N GLY D 47 47.243 44.993 32.219 1.000 29.82 ATOM 5859 CA GLY D 47 47.540 44.036 33.276 1.000 31.13 ATOM 5860 C GLY D 47 46.400 43.836 34.250 1.000 30.46 ATOM 5861 O GLY D 47 46.091 42.704 34.629 1.000 29.55 ATOM 5862 N GLU D 48 45.764 44.926 34.673 1.000 31.20 ATOM 5863 CA GLU D 48 44.610 44.847 35.571 1.000 30.44 ATOM 5864 CE GLU D 48 44.007 46.232 35.788 1.000 34.81 ATOM 5865 CG GLU D 48 42.910 46.303 36.839 1.000 46.31 ATOM 5866 CD GLU D 48 43.264 45.576 38.121 1.000 57.55 ATOM 5867 OE1 GLU D 48 42.788 44.440 38.332 1.000 64.75 ATOM 5868 OE2 GLU D 48 44.023 46.137 38.941 1.000 70.34 ATOM 5869 C GLU D 48 43.578 43.881 35.000 1.000 31.02 ATOM 5870 O GLU D 48 43.094 42.976 35.674 1.000 32.79 ATOM 5871 N ALA D 49 43.253 44.080 33.719 1.000 31.35 ATOM 5872 CA ALA D 49 42.284 43.191 33.085 1.000 32.00 ATOM 5873 CE ALA D 49 41.990 43.667 31.667 1.000 32.18 ATOM 5874 C ALA D 49 42.772 41.751 33.072 1.000 30.17 ATOM 5875 O ALA D 49 41.971 40.815 33.149 1.000 23.01 ATOM 5876 N GLN D 50 44.091 41.551 32.957 1.000 28.22 ATOM 5877 CA GLN D 50 44.565 40.162 32.932 1.000 27.11 ATOM 5878 CE GLN D 50 45.975 40.035 32.359 1.000 27.94 ATOM 5879 CG GLN D 50 46.147 40.500 30.926 1.000 27.74 ATOM 5880 CD GLN D 50 45.418 39.660 29.904 1.000 32.10 ATOM 5881 OE1 GLN D 50 45.275 40.065 28.743 1.000 48.53 ATOM 5882 NE2 GLN D 50 44.946 38.480 30.284 1.000 25.90 ATOM 5883 C GLN D 50 44.521 39.579 34.341 1.000 24.98 ATOM 5884 O GLN D 50 44.135 38.425 34.537 1.000 29.20 ATOM 5885 N ALA D 51 44.917 40.376 35.331 1.000 25.27 ATOM 5886 CA ALA D 51 44.834 39.906 36.715 1.000 28.77 ATOM 5887 CB ALA D 51 45.420 40.936 37.659 1.000 27.87 ATOM 5888 C ALA D 51 43.385 39.585 37.072 1.000 31.97 ATOM 5889 O ALA D 51 43.079 38.543 37.656 1.000 29.01 ATOM 5890 N LYS D 52 42.464 40.482 36.699 1.000 29.02 ATOM 5891 CA LYS D 52 41.060 40.239 37.044 1.000 33.68 ATOM 5892 CE LYS D 52 40.197 41.411 36.587 1.000 40.45 ATOM 5893 CG LYS D 52 38.775 41.054 36.190 1.000 51.10 ATOM 5894 CD LYS D 52 38.480 41.572 34.787 1.000 61.95 ATOM 5895 CE LYS D 52 38.743 40.511 33.728 1.000 61.99 ATOM 5896 NZ LYS D 52 39.088 41.105 32.407 1.000 39.68 ATOM 5897 C LYS D 52 40.579 38.918 36.457 1.000 32.76 ATOM 5898 O LYS D 52 39.896 38.129 37.111 1.000 30.38 ATOM 5899 N LYS D 53 40.949 38.658 35.205 1.000 31.19 ATOM 5900 CA LYS D 53 40.590 37.407 34.564 1.000 32.46 ATOM 5901 CE LYS D 53 41.041 37.418 33.103 1.000 35.74 ATOM 5902 C LYS D 53 41.200 36.197 35.253 1.000 35.48 ATOM 5903 O LYS D 53 40.652 35.092 35.205 1.000 38.08 ATOM 5904 N LEU D 54 42.362 36.356 35.893 1.000 36.19 ATOM 5905 CA LEU D 54 43.025 35.150 36.405 1.000 33.49 ATOM 5906 CE LEU D 54 44.546 35.358 36.360 1.000 29.70 ATOM 5907 CG LEU D 54 45.159 35.051 34.981 1.000 27.61 ATOM 5908 CD1 LEU D 54 46.577 35.580 34.901 1.000 29.55 ATOM 5909 CD2 LEU D 54 45.092 33.561 34.695 1.000 28.19 ATOM 5910 C LEU D 54 42.555 34.759 37.792 1.000 31.35 ATOM 5911 O LEU D 54 42.955 33.725 38.330 1.000 37.80 ATOM 5912 N GLY D 55 41.686 35.562 38.406 1.000 34.60 ATOM 5913 CA GLY D 55 41.066 35.155 39.655 1.000 30.33 ATOM 5914 C GLY D 55 41.688 35.717 40.911 1.000 29.00 ATOM 5915 O GLY D 55 42.597 36.540 40.837 1.000 24.79 ATOM 5916 N ASN D 56 41.193 35.276 42.067 1.000 32.09 ATOM 5917 CA ASN D 56 41.627 35.767 43.363 1.000 38.75 ATOM 5918 CB ASN D 56 40.961 34.951 44.486 1.000 45.97 ATOM 5919 CG ASN D 56 39.487 35.267 44.619 1.000 51.94 ATOM 5920 OD1 ASN D 56 38.654 34.375 44.752 1.000 60.92 ATOM 5921 ND2 ASN D 56 39.196 36.563 44.586 1.000 52.08 ATOM 5922 C ASN D 56 43.133 35.681 43.581 1.000 35.02 ATOM 5923 O ASN D 56 43.683 36.439 44.372 1.000 37.38 ATOM 5924 N ASN D 57 43.777 34.739 42.899 1.000 36.49 ATOM 5925 CA ASN D 57 45.174 34.441 43.206 1.000 34.75 ATOM 5926 CB ASN D 57 45.380 32.927 43.173 1.000 32.81 ATOM 5927 CG ASN D 57 44.745 32.237 44.369 1.000 38.51 ATOM 5928 OD1 ASN D 57 44.193 31.141 44.258 1.000 46.63 ATOM 5929 ND2 ASN D 57 44.829 32.884 45.527 1.000 40.21 ATOM 5930 C ASN D 57 46.131 35.146 42.257 1.000 35.44 ATOM 5931 O ASN D 57 47.289 34.760 42.091 1.000 31.41 ATOM 5932 N CYS D 58 45.653 36.206 41.621 1.000 32.36 ATOM 5933 CA CYS D 58 46.481 37.022 40.743 1.000 29.88 ATOM 5934 CB CYS D 58 46.313 36.559 39.291 1.000 28.72 ATOM 5935 SG CYS D 58 47.357 37.481 38.125 1.000 29.29 ATOM 5936 C CYS D 58 46.128 38.494 40.875 1.000 27.06 ATOM 5937 O CYS D 58 44.974 38.899 40.701 1.000 27.89 ATOM 5938 N VAL D 59 47.097 39.347 41.185 1.000 26.91 ATOM 5939 CA VAL D 59 46.804 40.781 41.220 1.000 28.98 ATOM 5940 CB VAL D 59 46.808 41.346 42.650 1.000 32.06 ATOM 5941 CG1 VAL D 59 45.829 40.568 43.524 1.000 34.22 ATOM 5942 CG2 VAL D 59 48.215 41.316 43.222 1.000 31.06 ATOM 5943 C VAL D 59 47.810 41.570 40.383 1.000 31.95 ATOM 5944 O VAL D 59 48.907 41.095 40.090 1.000 29.89 ATOM 5945 N PHE D 60 47.420 42.780 40.006 1.000 28.61 ATOM 5946 CA PHE D 60 48.225 43.643 39.154 1.000 28.36 ATOM 5947 CB PHE D 60 47.342 44.259 38.061 1.000 26.03 ATOM 5948 CG PHE D 60 48.022 45.361 37.268 1.000 26.77 ATOM 5949 CD1 PHE D 60 49.131 45.076 36.490 1.000 31.57 ATOM 5950 CD2 PHE D 60 47.566 46.662 37.297 1.000 28.37 ATOM 5951 CE1 PHE D 60 49.760 46.071 35.759 1.000 29.22 ATOM 5952 CE2 PHE D 60 48.181 47.668 36.574 1.000 28.34 ATOM 5953 CZ PHE D 60 49.287 47.371 35.802 1.000 27.71 ATOM 5954 C PHE D 60 48.910 44.731 39.970 1.000 30.78 ATOM 5955 O PHE D 60 48.294 45.377 40.816 1.000 25.79 ATOM 5956 N ALA D 61 50.196 44.935 39.715 1.000 28.24 ATOM 5957 CA ALA D 61 50.955 46.014 40.331 1.000 25.80 ATOM 5958 CB ALA D 61 52.099 45.458 41.164 1.000 27.20 ATOM 5959 C ALA D 61 51.485 46.952 39.252 1.000 26.85 ATOM 5960 O ALA D 61 52.432 46.595 38.549 1.000 30.94 ATOM 5961 N PRO D 62 50.896 48.131 39.111 1.000 29.26 ATOM 5962 CD PRO D 62 49.790 48.672 39.919 1.000 24.84 ATOM 5963 CA PRO D 62 51.336 49.068 38.070 1.000 27.67 ATOM 5964 CB PRO D 62 50.329 50.217 38.185 1.000 28.36 ATOM 5965 CG PRO D 62 49.837 50.141 39.597 1.000 28.36 ATOM 5966 C PRO D 62 52.739 49.588 38.345 1.000 29.75 ATOM 5967 O PRO D 62 53.019 50.135 39.416 1.000 30.01 ATOM 5968 N ALA D 63 53.667 49.441 37.401 1.000 26.51 ATOM 5969 CA ALA D 63 55.017 49.923 37.679 1.000 27.47 ATOM 5970 CB ALA D 63 55.634 49.131 38.832 1.000 24.94 ATOM 5971 C ALA D 63 55.933 49.840 36.456 1.000 22.74 ATOM 5972 O ALA D 63 55.773 48.942 35.634 1.000 22.77 ATOM 5973 N ASP D 64 56.862 50.775 36.406 1.000 22.65 ATOM 5974 CA ASP D 64 57.968 50.830 35.458 1.000 26.50 ATOM 5975 CB ASP D 64 58.212 52.271 35.037 1.000 21.81 ATOM 5976 CG ASP D 64 59.270 52.434 33.969 1.000 28.32 ATOM 5977 OD1 ASP D 64 59.229 53.472 33.272 1.000 33.50 ATOM 5978 OD2 ASP D 64 60.140 51.549 33.820 1.000 29.49 ATOM 5979 C ASP D 64 59.214 50.235 36.107 1.000 25.03 ATOM 5980 O ASP D 64 59.679 50.774 37.112 1.000 22.61 ATOM 5981 N VAL D 65 59.758 49.150 35.574 1.000 27.71 ATOM 5982 CA VAL D 65 60.893 48.476 36.207 1.000 25.12 ATOM 5983 CB VAL D 65 61.241 47.133 35.540 1.000 20.68 ATOM 5984 CG1 VAL D 65 60.113 46.122 35.682 1.000 16.74 ATOM 5985 CG2 VAL D 65 61.566 47.314 34.065 1.000 23.11 ATOM 5986 C VAL D 65 62.136 49.356 36.230 1.000 23.46 ATOM 5987 O VAL D 65 63.080 49.064 36.976 1.000 25.73 ATOM 5988 N THR D 66 62.195 50.444 35.460 1.000 19.65 ATOM 5989 CA THR D 66 63.362 51.313 35.578 1.000 20.93 ATOM 5990 CB THR D 66 63.553 52.221 34.349 1.000 24.85 ATOM 5991 OG1 THR D 66 62.389 53.045 34.196 1.000 27.53 ATOM 5992 CG2 THR D 66 63.691 51.407 33.076 1.000 27.72 ATOM 5993 C THR D 66 63.272 52.221 36.803 1.000 27.29 ATOM 5994 O THR D 66 64.143 53.067 37.028 1.000 26.24 ATOM 5995 N SER D 67 62.208 52.064 37.593 1.000 27.60 ATOM 5996 CA SER D 67 61.987 52.986 38.698 1.000 27.65 ATOM 5997 CB SER D 67 60.599 53.649 38.564 1.000 24.23 ATOM 5998 OG SER D 67 60.362 54.377 39.765 1.000 29.46 ATOM 5999 C SER D 67 62.083 52.320 40.063 1.000 24.57 ATOM 6000 O SER D 67 61.375 51.358 40.341 1.000 25.87 ATOM 6001 N GLU D 68 62.947 52.826 40.930 1.000 27.01 ATOM 6002 CA GLU D 68 63.092 52.281 42.277 1.000 28.26 ATOM 6003 CB GLU D 68 64.172 53.068 43.020 1.000 29.92 ATOM 6004 CG GLU D 68 64.439 52.624 44.449 1.000 33.31 ATOM 6005 CD GLU D 68 65.710 53.252 45.002 1.000 37.25 ATOM 6006 OE1 GLU D 68 66.756 52.568 45.036 1.000 34.88 ATOM 6007 OE2 GLU D 68 65.671 54.437 45.393 1.000 42.89 ATOM 6008 C GLU D 68 61.772 52.340 43.036 1.000 26.65 ATOM 6009 O GLU D 68 61.299 51.352 43.598 1.000 22.12 ATOM 6010 N LYS D 69 61.174 53.533 43.037 1.000 21.31 ATOM 6011 CA LYS D 69 59.927 53.743 43.769 1.000 27.84 ATOM 6012 CB LYS D 69 59.507 55.207 43.685 1.000 33.93 ATOM 6013 C LYS D 69 58.813 52.832 43.275 1.000 29.51 ATOM 6014 O LYS D 69 58.129 52.184 44.075 1.000 28.88 ATOM 6015 N ASP D 70 58.619 52.756 41.961 1.000 24.87 ATOM 6016 CA ASP D 70 57.585 51.889 41.411 1.000 28.61 ATOM 6017 CB ASP D 70 57.550 51.965 39.883 1.000 31.79 ATOM 6018 CG ASP D 70 56.975 53.251 39.331 1.000 30.51 ATOM 6019 OD1 ASP D 70 56.695 54.179 40.118 1.000 32.19 ATOM 6020 OD2 ASP D 70 56.817 53.319 38.093 1.000 29.00 ATOM 6021 C ASP D 70 57.799 50.435 41.805 1.000 25.20 ATOM 6022 O ASP D 70 56.881 49.687 42.137 1.000 28.32 ATOM 6023 N VAL D 71 59.060 49.986 41.755 1.000 26.27 ATOM 6024 CA VAL D 71 59.277 48.575 42.094 1.000 23.48 ATOM 6025 CB VAL D 71 60.668 48.105 41.660 1.000 25.09 ATOM 6026 CG1 VAL D 71 60.897 46.670 42.096 1.000 21.61 ATOM 6027 CG2 VAL D 71 60.808 48.237 40.144 1.000 30.05 ATOM 6028 C VAL D 71 59.064 48.376 43.590 1.000 23.38 ATOM 6029 O VAL D 71 58.490 47.379 44.032 1.000 24.10 ATOM 6030 N GLN D 72 59.526 49.361 44.370 1.000 23.68 ATOM 6031 CA GLN D 72 59.295 49.251 45.817 1.000 29.60 ATOM 6032 CB GLN D 72 59.922 50.435 46.543 1.000 27.41 ATOM 6033 CG GLN D 72 61.441 50.369 46.601 1.000 30.50 ATOM 6034 CD GLN D 72 62.070 51.677 47.037 1.000 36.83 ATOM 6035 OE1 GLN D 72 61.498 52.751 46.847 1.000 42.88 ATOM 6036 NE2 GLN D 72 63.258 51.588 47.626 1.000 40.04 ATOM 6037 C GLN D 72 57.800 49.156 46.082 1.000 25.91 ATOM 6038 O GLN D 72 57.298 48.323 46.823 1.000 29.83 ATOM 6039 N THR D 73 57.042 50.033 45.418 1.000 26.69 ATOM 6040 CA THR D 73 55.589 49.988 45.579 1.000 28.25 ATOM 6041 CB THR D 73 54.934 51.109 44.755 1.000 35.55 ATOM 6042 OG1 THR D 73 55.318 52.363 45.340 1.000 37.75 ATOM 6043 CG2 THR D 73 53.419 51.024 44.814 1.000 36.99 ATOM 6044 C THR D 73 55.025 48.643 45.176 1.000 32.13 ATOM 6045 O THR D 73 54.256 48.009 45.909 1.000 38.91 ATOM 6046 N ALA D 74 55.384 48.152 43.988 1.000 26.62 ATOM 6047 CA ALA D 74 54.786 46.877 43.587 1.000 22.02 ATOM 6048 CB ALA D 74 55.130 46.562 42.135 1.000 26.82 ATOM 6049 C ALA D 74 55.216 45.759 44.519 1.000 25.59 ATOM 6050 O ALA D 74 54.449 44.827 44.777 1.000 33.16 ATOM 6051 N LEU D 75 56.434 45.794 45.066 1.000 25.61 ATOM 6052 CA LEU D 75 56.769 44.677 45.966 1.000 27.99 ATOM 6053 CB LEU D 75 58.271 44.644 46.246 1.000 28.13 ATOM 6054 CG LEU D 75 59.134 44.234 45.044 1.000 26.15 ATOM 6055 CD1 LEU D 75 60.612 44.405 45.366 1.000 27.79 ATOM 6056 CD2 LEU D 75 58.822 42.805 44.640 1.000 21.18 ATOM 6057 C LEU D 75 55.975 44.769 47.269 1.000 26.60 ATOM 6058 O LEU D 75 55.493 43.758 47.778 1.000 26.29 ATOM 6059 N ALA D 76 55.826 45.973 47.811 1.000 25.68 ATOM 6060 CA ALA D 76 55.045 46.128 49.042 1.000 33.09 ATOM 6061 CB ALA D 76 55.104 47.564 49.541 1.000 31.43 ATOM 6062 C ALA D 76 53.603 45.692 48.819 1.000 37.27 ATOM 6063 O ALA D 76 52.960 45.065 49.666 1.000 35.63 ATOM 6064 N LEU D 77 53.078 46.023 47.639 1.000 36.38 ATOM 6065 CA LEU D 77 51.740 45.556 47.265 1.000 29.31 ATOM 6066 CB LEU D 77 51.398 46.024 45.856 1.000 33.44 ATOM 6067 CG LEU D 77 49.932 46.072 45.431 1.000 38.05 ATOM 6068 CD1 LEU D 77 49.777 47.044 44.263 1.000 38.40 ATOM 6069 CD2 LEU D 77 49.396 44.700 45.059 1.000 30.81 ATOM 6070 C LEU D 77 51.689 44.041 47.351 1.000 31.64 ATOM 6071 O LEU D 77 50.752 43.432 47.855 1.000 36.47 ATOM 6072 N ALA D 78 52.756 43.408 46.848 1.000 31.80 ATOM 6073 CA ALA D 78 52.815 41.950 46.860 1.000 34.05 ATOM 6074 CB ALA D 78 54.036 41.462 46.087 1.000 31.79 ATOM 6075 C ALA D 78 52.847 41.404 48.281 1.000 29.19 ATOM 6076 O ALA D 78 52.165 40.436 48.622 1.000 26.82 ATOM 6077 N LYS D 79 53.680 42.016 49.119 1.000 30.72 ATOM 6078 CA LYS D 79 53.809 41.519 50.488 1.000 35.21 ATOM 6079 CB LYS D 79 54.853 42.314 51.247 1.000 32.89 ATOM 6080 C LYS D 79 52.449 41.576 51.185 1.000 38.85 ATOM 6081 O LYS D 79 52.023 40.609 51.809 1.000 35.65 ATOM 6082 N GLY D 80 51.800 42.728 51.047 1.000 39.97 ATOM 6083 CA GLY D 80 50.507 42.973 51.649 1.000 40.46 ATOM 6084 C GLY D 80 49.414 42.076 51.129 1.000 42.76 ATOM 6085 O GLY D 80 48.458 41.739 51.836 1.000 41.31 ATOM 6086 N LYS D 81 49.502 41.656 49.864 1.000 36.98 ATOM 6087 CA LYS D 81 48.411 40.821 49.363 1.000 34.65 ATOM 6088 CB LYS D 81 48.184 41.075 47.868 1.000 38.61 ATOM 6089 CG LYS D 81 47.306 40.047 47.182 1.000 46.80 ATOM 6090 CD LYS D 81 45.842 40.198 47.558 1.000 53.26 ATOM 6091 CE LYS D 81 45.053 38.941 47.237 1.000 57.99 ATOM 6092 NZ LYS D 81 43.619 39.237 46.954 1.000 62.28 ATOM 6093 C LYS D 81 48.675 39.350 49.631 1.000 36.61 ATOM 6094 O LYS D 81 47.745 38.577 49.879 1.000 35.63 ATOM 6095 N PHE D 82 49.939 38.922 49.579 1.000 32.32 ATOM 6096 CA PHE D 82 50.180 37.487 49.705 1.000 30.51 ATOM 6097 CB PHE D 82 50.694 36.929 48.365 1.000 34.03 ATOM 6098 CG PHE D 82 49.646 37.028 47.262 1.000 33.10 ATOM 6099 CD1 PHE D 82 48.471 36.303 47.370 1.000 30.63 ATOM 6100 CD2 PHE D 82 49.839 37.838 46.156 1.000 28.41 ATOM 6101 CE1 PHE D 82 47.500 36.390 46.390 1.000 34.05 ATOM 6102 CE2 PHE D 82 48.877 37.925 45.167 1.000 29.55 ATOM 6103 CZ PHE D 82 47.707 37.198 45.288 1.000 34.23 ATOM 6104 C PHE D 82 51.160 37.149 50.815 1.000 31.92 ATOM 6105 O PHE D 82 51.437 35.967 51.032 1.000 35.21 ATOM 6106 N GLY D 83 51.683 38.153 51.506 1.000 33.75 ATOM 6107 CA GLY D 83 52.547 37.968 52.646 1.000 37.01 ATOM 6108 C GLY D 83 54.012 37.721 52.376 1.000 41.28 ATOM 6109 O GLY D 83 54.848 37.931 53.263 1.000 37.16 ATOM 6110 N ARG D 84 54.365 37.263 51.176 1.000 37.51 ATOM 6111 CA ARG D 84 55.746 36.920 50.867 1.000 32.37 ATOM 6112 CB ARG D 84 56.147 35.583 51.493 1.000 27.65 ATOM 6113 CG ARG D 84 55.156 34.453 51.321 1.000 34.94 ATOM 6114 CD ARG D 84 55.813 33.082 51.292 1.000 43.12 ATOM 6115 NE ARG D 84 56.425 32.711 52.553 1.000 51.85 ATOM 6116 CZ ARG D 84 57.511 31.989 52.773 1.000 56.19 ATOM 6117 NE1 ARG D 84 57.895 31.773 54.028 1.000 62.19 ATOM 6118 NH2 ARG D 84 58.221 31.477 51.772 1.000 34.76 ATOM 6119 C ARG D 84 55.960 36.869 49.354 1.000 33.88 ATOM 6120 O ARG D 84 55.003 36.941 48.589 1.000 35.01 ATOM 6121 N VAL D 85 57.219 36.758 48.954 1.000 29.87 ATOM 6122 CA VAL D 85 57.626 36.532 47.576 1.000 26.11 ATOM 6123 CB VAL D 85 58.282 37.762 46.934 1.000 28.50 ATOM 6124 CG1 VAL D 85 58.505 37.488 45.447 1.000 29.52 ATOM 6125 CG2 VAL D 85 57.442 39.012 47.126 1.000 25.93 ATOM 6126 C VAL D 85 58.604 35.356 47.510 1.000 25.14 ATOM 6127 O VAL D 85 59.683 35.397 48.102 1.000 25.12 ATOM 6128 N ASP D 86 58.218 34.306 46.803 1.000 25.70 ATOM 6129 CA ASP D 86 58.998 33.093 46.654 1.000 24.79 ATOM 6130 CE ASP D 86 58.104 31.850 46.759 1.000 26.03 ATOM 6131 CG ASP D 86 57.298 31.824 48.045 1.000 31.97 ATOM 6132 OD1 ASP D 86 56.057 31.880 47.996 1.000 31.52 ATOM 6133 OD2 ASP D 86 57.903 31.755 49.137 1.000 34.74 ATOM 6134 C ASP D 86 59.723 33.039 45.309 1.000 29.22 ATOM 6135 O ASP D 86 60.778 32.410 45.217 1.000 24.49 ATOM 6136 N VAL D 87 59.153 33.674 44.288 1.000 21.53 ATOM 6137 CA VAL D 87 59.718 33.601 42.941 1.000 21.23 ATOM 6138 CB VAL D 87 58.939 32.574 42.089 1.000 26.73 ATOM 6139 CG1 VAL D 87 59.413 32.610 40.639 1.000 25.47 ATOM 6140 CG2 VAL D 87 59.064 31.172 42.670 1.000 24.94 ATOM 6141 C VAL D 87 59.664 34.939 42.222 1.000 24.90 ATOM 6142 O VAL D 87 58.639 35.624 42.292 1.000 27.16 ATOM 6143 N ALA D 88 60.734 35.313 41.521 1.000 22.93 ATOM 6144 CA ALA D 88 60.677 36.485 40.646 1.000 22.19 ATOM 6145 CB ALA D 88 61.602 37.591 41.104 1.000 17.29 ATOM 6146 C ALA D 88 60.993 36.071 39.203 1.000 24.09 ATOM 6147 O ALA D 88 61.921 35.296 38.964 1.000 23.46 ATOM 6148 N VAL D 89 60.197 36.577 38.274 1.000 20.82 ATOM 6149 CA VAL D 89 60.382 36.313 36.850 1.000 21.18 ATOM 6150 CE VAL D 89 59.299 35.426 36.219 1.000 27.30 ATOM 6151 CG1 VAL D 89 59.716 35.012 34.810 1.000 18.72 ATOM 6152 CG2 VAL D 89 58.998 34.168 37.028 1.000 15.99 ATOM 6153 C VAL D 89 60.414 37.654 36.116 1.000 22.82 ATOM 6154 O VAL D 89 59.413 38.373 36.103 1.000 24.02 ATOM 6155 N ASN D 90 61.565 37.980 35.539 1.000 20.51 ATOM 6156 CA ASN D 90 61.733 39.203 34.774 1.000 20.17 ATOM 6157 CB ASN D 90 63.161 39.739 34.930 1.000 19.28 ATOM 6158 CG ASN D 90 63.473 40.175 36.344 1.000 21.33 ATOM 6159 OD1 ASN D 90 64.242 39.531 37.061 1.000 24.72 ATOM 6160 ND2 ASN D 90 62.896 41.282 36.769 1.000 17.80 ATOM 6161 C ASN D 90 61.417 38.960 33.297 1.000 24.77 ATOM 6162 O ASN D 90 62.168 38.277 32.594 1.000 26.87 ATOM 6163 N CYS D 91 60.310 39.511 32.807 1.000 23.72 ATOM 6164 CA CYS D 91 59.947 39.394 31.401 1.000 23.76 ATOM 6165 CB CYS D 91 58.650 38.599 31.207 1.000 17.89 ATOM 6166 SG CYS D 91 58.869 36.834 31.517 1.000 25.59 ATOM 6167 C CYS D 91 59.815 40.766 30.749 1.000 26.58 ATOM 6168 O CYS D 91 59.791 40.871 29.515 1.000 21.51 ATOM 6169 N ALA D 92 59.755 41.811 31.566 1.000 21.43 ATOM 6170 CA ALA D 92 59.687 43.167 31.039 1.000 23.48 ATOM 6171 CB ALA D 92 59.741 44.198 32.158 1.000 15.96 ATOM 6172 C ALA D 92 60.820 43.419 30.046 1.000 29.54 ATOM 6173 O ALA D 92 61.996 43.186 30.345 1.000 22.45 ATOM 6174 N GLY D 93 60.480 43.905 28.853 1.000 26.21 ATOM 6175 CA GLY D 93 61.520 44.147 27.865 1.000 20.92 ATOM 6176 C GLY D 93 61.011 44.826 26.608 1.000 26.44 ATOM 6177 O GLY D 93 59.832 44.733 26.267 1.000 21.58 ATOM 6178 N ILE D 94 61.915 45.504 25.908 1.000 22.55 ATOM 6179 CA ILE D 94 61.599 46.146 24.644 1.000 22.55 ATOM 6180 CB ILE D 94 61.573 47.682 24.730 1.000 22.02 ATOM 6181 CG2 ILE D 94 60.365 48.150 25.521 1.000 23.98 ATOM 6182 CG1 ILE D 94 62.885 48.264 25.259 1.000 23.94 ATOM 6183 CD1 ILE D 94 63.023 49.759 25.097 1.000 26.35 ATOM 6184 C ILE D 94 62.642 45.766 23.586 1.000 25.24 ATOM 6185 O ILE D 94 63.715 45.245 23.892 1.000 17.15 ATOM 6186 N ALA D 95 62.279 46.051 22.345 1.000 30.45 ATOM 6187 CA ALA D 95 63.094 45.746 21.183 1.000 29.43 ATOM 6188 CE ALA D 95 62.431 44.635 20.377 1.000 25.68 ATOM 6189 C ALA D 95 63.289 46.976 20.312 1.000 31.25 ATOM 6190 O ALA D 95 62.416 47.841 20.228 1.000 26.09 ATOM 6191 N VAL D 96 64.447 47.066 19.662 1.000 27.30 ATOM 6192 CA VAL D 96 64.634 48.064 18.625 1.000 25.24 ATOM 6193 CB VAL D 96 65.327 49.365 19.058 1.000 36.51 ATOM 6194 CG1 VAL D 96 64.693 49.957 20.306 1.000 52.71 ATOM 6195 CG2 VAL D 96 66.817 49.129 19.280 1.000 41.65 ATOM 6196 C VAL D 96 65.470 47.431 17.506 1.000 25.45 ATOM 6197 O VAL D 96 66.282 46.535 17.727 1.000 21.54 ATOM 6198 N ALA D 97 65.243 47.926 16.299 1.000 21.06 ATOM 6199 CA ALA D 97 66.067 47.468 15.176 1.000 21.96 ATOM 6200 CE ALA D 97 65.236 46.724 14.157 1.000 27.78 ATOM 6201 C ALA D 97 66.751 48.710 14.617 1.000 24.35 ATOM 6202 O ALA D 97 66.062 49.615 14.147 1.000 27.82 ATOM 6203 N SER D 98 68.074 48.763 14.702 1.000 21.21 ATOM 6204 CA SER D 98 68.799 49.939 14.223 1.000 25.16 ATOM 6205 CE SER D 98 68.582 51.111 15.175 1.000 22.16 ATOM 6206 OG SER D 98 69.228 52.299 14.765 1.000 23.19 ATOM 6207 C SER D 98 70.278 49.604 14.069 1.000 27.15 ATOM 6208 O SER D 98 70.929 49.216 15.042 1.000 21.76 ATOM 6209 N LYS D 99 70.792 49.761 12.854 1.000 21.91 ATOM 6210 CA LYS D 99 72.201 49.518 12.579 1.000 24.27 ATOM 6211 CE LYS D 99 72.471 49.620 11.070 1.000 24.05 ATOM 6212 CG LYS D 99 71.911 48.450 10.278 1.000 24.66 ATOM 6213 CD LYS D 99 71.701 48.833 8.820 1.000 31.29 ATOM 6214 CE LYS D 99 71.044 47.714 8.034 1.000 36.32 ATOM 6215 NZ LYS D 99 71.644 47.527 6.685 1.000 50.21 ATOM 6216 C LYS D 99 73.128 50.488 13.304 1.000 24.08 ATOM 6217 O LYS D 99 72.824 51.672 13.449 1.000 21.85 ATOM 6218 N THR D 100 74.282 49.979 13.746 1.000 19.95 ATOM 6219 CA THR D 100 75.254 50.836 14.422 1.000 19.55 ATOM 6220 CB THR D 100 76.545 50.079 14.781 1.000 21.22 ATOM 6221 OG1 THR D 100 76.257 48.985 15.655 1.000 24.03 ATOM 6222 CG2 THR D 100 77.466 51.030 15.532 1.000 22.24 ATOM 6223 C THR D 100 75.622 52.043 13.566 1.000 21.15 ATOM 6224 O THR D 100 75.636 53.187 14.026 1.000 19.49 ATOM 6225 N TYR D 101 75.917 51.761 12.299 1.000 20.95 ATOM 6226 CA TYR D 101 76.167 52.806 11.312 1.000 22.24 ATOM 6227 CB TYR D 101 77.625 53.287 11.272 1.000 23.19 ATOM 6228 CG TYR D 101 77.835 54.290 10.152 1.000 24.99 ATOM 6229 CD1 TYR D 101 78.536 53.962 9.004 1.000 30.17 ATOM 6230 CE1 TYR D 101 78.715 54.887 7.989 1.000 33.21 ATOM 6231 CD2 TYR D 101 77.308 55.568 10.251 1.000 29.66 ATOM 6232 CE2 TYR D 101 77.474 56.503 9.247 1.000 29.30 ATOM 6233 CZ TYR D 101 78.180 56.150 8.118 1.000 34.03 ATOM 6234 OH TYR D 101 78.352 57.072 7.109 1.000 33.32 ATOM 6235 C TYR D 101 75.754 52.275 9.940 1.000 29.72 ATOM 6236 O TYR D 101 76.075 51.134 9.609 1.000 26.97 ATOM 6237 N ASN D 102 75.036 53.098 9.185 1.000 29.84 ATOM 6238 CA ASN D 102 74.534 52.672 7.879 1.000 27.82 ATOM 6239 CB ASN D 102 73.013 52.716 7.886 1.000 29.39 ATOM 6240 CG ASN D 102 72.379 52.247 6.594 1.000 37.37 ATOM 6241 OD1 ASN D 102 73.063 52.102 5.579 1.000 39.57 ATOM 6242 ND2 ASN D 102 71.070 52.010 6.634 1.000 26.10 ATOM 6243 C ASN D 102 75.118 53.566 6.792 1.000 27.53 ATOM 6244 O ASN D 102 74.664 54.693 6.601 1.000 28.16 ATOM 6245 N LEU D 103 76.145 53.089 6.092 1.000 30.38 ATOM 6246 CA LEU D 103 76.778 53.927 5.077 1.000 32.06 ATOM 6247 CB LEU D 103 78.029 53.267 4.499 1.000 31.44 ATOM 6248 CG LEU D 103 78.845 54.165 3.556 1.000 31.02 ATOM 6249 CD1 LEU D 103 79.382 55.382 4.291 1.000 34.86 ATOM 6250 CD2 LEU D 103 79.975 53.376 2.910 1.000 31.19 ATOM 6251 C LEU D 103 75.799 54.252 3.951 1.000 38.73 ATOM 6252 O LEU D 103 75.758 55.382 3.458 1.000 41.00 ATOM 6253 N LYS D 104 75.006 53.256 3.568 1.000 42.41 ATOM 6254 CA LYS D 104 74.059 53.402 2.469 1.000 42.43 ATOM 6255 CB LYS D 104 73.257 52.117 2.304 1.000 49.29 ATOM 6256 C LYS D 104 73.135 54.594 2.672 1.000 38.48 ATOM 6257 O LYS D 104 72.873 55.374 1.758 1.000 46.32 ATOM 6258 N LYS D 105 72.629 54.738 3.882 1.000 34.33 ATOM 6259 CA LYS D 105 71.759 55.831 4.272 1.000 34.50 ATOM 6260 CB LYS D 105 70.730 55.320 5.280 1.000 43.73 ATOM 6261 CG LYS D 105 69.341 55.017 4.762 1.000 51.53 ATOM 6262 CD LYS D 105 68.334 55.177 5.902 1.000 60.99 ATOM 6263 CE LYS D 105 68.852 56.167 6.937 1.000 66.55 ATOM 6264 NZ LYS D 105 68.589 55.715 8.329 1.000 70.72 ATOM 6265 C LYS D 105 72.544 56.954 4.927 1.000 31.68 ATOM 6266 O LYS D 105 71.971 57.994 5.265 1.000 34.61 ATOM 6267 N GLY D 106 73.844 56.744 5.149 1.000 26.87 ATOM 6268 CA GLY D 106 74.599 57.744 5.902 1.000 24.09 ATOM 6269 C GLY D 106 73.997 57.951 7.281 1.000 29.52 ATOM 6270 O GLY D 106 73.940 59.070 7.794 1.000 36.21 ATOM 6271 N GLN D 107 73.531 56.873 7.908 1.000 31.56 ATOM 6272 CA GLN D 107 72.821 56.986 9.176 1.000 31.60 ATOM 6273 CB GLN D 107 71.414 56.420 9.023 1.000 31.54 ATOM 6274 C GLN D 107 73.535 56.282 10.326 1.000 27.83 ATOM 6275 O GLN D 107 74.124 55.221 10.139 1.000 21.99 ATOM 6276 N THR D 108 73.450 56.914 11.488 1.000 28.97 ATOM 6277 CA THR D 108 74.099 56.498 12.718 1.000 27.95 ATOM 6278 CB THR D 108 75.039 57.610 13.230 1.000 27.01 ATOM 6279 OG1 THR D 108 76.069 57.806 12.244 1.000 26.81 ATOM 6280 CG2 THR D 108 75.712 57.203 14.535 1.000 23.92 ATOM 6281 C THR D 108 73.093 56.158 13.813 1.000 25.94 ATOM 6282 O THR D 108 72.169 56.930 14.057 1.000 24.57 ATOM 6283 N HIS D 109 73.288 55.017 14.460 1.000 24.99 ATOM 6284 CA HIS D 109 72.481 54.609 15.610 1.000 22.08 ATOM 6285 CB HIS D 109 73.066 53.330 16.199 1.000 24.31 ATOM 6286 CG HIS D 109 72.217 52.581 17.173 1.000 21.11 ATOM 6287 CD2 HIS D 109 71.849 51.281 17.199 1.000 22.29 ATOM 6288 ND1 HIS D 109 71.647 53.161 18.289 1.000 21.14 ATOM 6289 CE1 HIS D 109 70.961 52.248 18.953 1.000 22.36 ATOM 6290 NE2 HIS D 109 71.064 51.090 18.313 1.000 24.23 ATOM 6291 C HIS D 109 72.442 55.727 16.634 1.000 21.13 ATOM 6292 O HIS D 109 73.475 56.295 16.997 1.000 24.86 ATOM 6293 N THR D 110 71.265 56.105 17.134 1.000 22.33 ATOM 6294 CA THR D 110 71.270 57.195 18.113 1.000 21.15 ATOM 6295 CB THR D 110 69.891 57.855 18.291 1.000 24.47 ATOM 6296 OG1 THR D 110 69.064 56.917 19.003 1.000 24.44 ATOM 6297 CG2 THR D 110 69.245 58.154 16.947 1.000 22.97 ATOM 6298 C THR D 110 71.697 56.698 19.488 1.000 22.11 ATOM 6299 O THR D 110 71.439 55.555 19.857 1.000 28.62 ATOM 6300 N LEU D 111 72.331 57.585 20.245 1.000 25.58 ATOM 6301 CA LEU D 111 72.736 57.213 21.601 1.000 24.13 ATOM 6302 CB LEU D 111 73.554 58.351 22.214 1.000 22.07 ATOM 6303 CG LEU D 111 74.351 58.004 23.473 1.000 27.10 ATOM 6304 CD1 LEU D 111 75.280 56.822 23.222 1.000 23.25 ATOM 6305 CD2 LEU D 111 75.156 59.199 23.966 1.000 26.98 ATOM 6306 C LEU D 111 71.519 56.871 22.448 1.000 25.93 ATOM 6307 O LEU D 111 71.495 55.918 23.234 1.000 25.17 ATOM 6308 N GLU D 112 70.447 57.654 22.311 1.000 24.62 ATOM 6309 CA GLU D 112 69.296 57.407 23.179 1.000 31.12 ATOM 6310 CB GLU D 112 68.320 58.590 23.145 1.000 42.68 ATOM 6311 CG GLU D 112 68.495 59.531 24.328 1.000 59.94 ATOM 6312 CD GLU D 112 69.326 58.988 25.477 1.000 63.78 ATOM 6313 OE1 GLU D 112 68.742 58.501 26.473 1.000 57.36 ATOM 6314 OE2 GLU D 112 70.577 59.055 25.393 1.000 40.17 ATOM 6315 C GLU D 112 68.584 56.108 22.842 1.000 29.53 ATOM 6316 O GLU D 112 68.017 55.506 23.759 1.000 27.04 ATOM 6317 N ASP D 113 68.608 55.665 21.591 1.000 26.11 ATOM 6318 CA ASP D 113 68.051 54.351 21.270 1.000 25.53 ATOM 6319 CB ASP D 113 68.096 54.113 19.759 1.000 25.99 ATOM 6320 CG ASP D 113 66.784 54.448 19.072 1.000 30.30 ATOM 6321 OD1 ASP D 113 65.844 54.914 19.753 1.000 32.37 ATOM 6322 OD2 ASP D 113 66.656 54.246 17.848 1.000 28.37 ATOM 6323 C ASP D 113 68.805 53.247 22.013 1.000 24.25 ATOM 6324 O ASP D 113 68.240 52.244 22.448 1.000 24.18 ATOM 6325 N PHE D 114 70.115 53.436 22.152 1.000 19.95 ATOM 6326 CA PHE D 114 70.939 52.464 22.872 1.000 22.83 ATOM 6327 CB PHE D 114 72.420 52.714 22.607 1.000 20.00 ATOM 6328 CG PHE D 114 73.343 51.605 23.067 1.000 22.08 ATOM 6329 CD1 PHE D 114 73.985 51.682 24.292 1.000 22.82 ATOM 6330 CD2 PHE D 114 73.561 50.494 22.270 1.000 21.94 ATOM 6331 CE1 PHE D 114 74.820 50.666 24.715 1.000 20.62 ATOM 6332 CE2 PHE D 114 74.398 49.476 22.680 1.000 21.46 ATOM 6333 CZ PHE D 114 75.039 49.576 23.899 1.000 18.59 ATOM 6334 C PHE D 114 70.643 52.534 24.372 1.000 21.87 ATOM 6335 O PHE D 114 70.464 51.496 25.009 1.000 21.31 ATOM 6336 N GLN D 115 70.583 53.743 24.913 1.000 24.02 ATOM 6337 CA GLN D 115 70.370 53.959 26.344 1.000 24.66 ATOM 6338 CB GLN D 115 70.477 55.444 26.700 1.000 25.07 ATOM 6339 CG GLN D 115 70.334 55.724 28.197 1.000 29.62 ATOM 6340 CD GLN D 115 71.606 55.421 28.961 1.000 32.26 ATOM 6341 OE1 GLN D 115 72.679 55.907 28.602 1.000 32.00 ATOM 6342 NE2 GLN D 115 71.525 54.622 30.019 1.000 29.01 ATOM 6343 C GLN D 115 69.016 53.433 26.802 1.000 22.64 ATOM 6344 O GLN D 115 68.895 52.844 27.871 1.000 26.88 ATOM 6345 N ARG D 116 67.982 53.648 25.998 1.000 21.99 ATOM 6346 CA ARG D 116 66.637 53.224 26.372 1.000 23.55 ATOM 6347 CB ARG D 116 65.640 53.763 25.350 1.000 27.00 ATOM 6348 C ARG D 116 66.532 51.711 26.504 1.000 23.39 ATOM 6349 O ARG D 116 65.906 51.149 27.406 1.000 21.70 ATOM 6350 N VAL D 117 67.144 50.989 25.573 1.000 21.56 ATOM 6351 CA VAL D 117 67.073 49.533 25.582 1.000 23.53 ATOM 6352 CB VAL D 117 67.609 48.990 24.239 1.000 22.11 ATOM 6353 CG1 VAL D 117 67.774 47.484 24.260 1.000 16.76 ATOM 6354 CG2 VAL D 117 66.664 49.411 23.115 1.000 26.84 ATOM 6355 C VAL D 117 67.846 48.937 26.753 1.000 20.88 ATOM 6356 O VAL D 117 67.446 47.933 27.343 1.000 22.24 ATOM 6357 N LEU D 118 68.975 49.539 27.087 1.000 18.85 ATOM 6358 CA LEU D 118 69.789 49.147 28.221 1.000 23.19 ATOM 6359 CB LEU D 118 71.041 50.009 28.348 1.000 23.72 ATOM 6360 CG LEU D 118 72.317 49.661 27.600 1.000 37.64 ATOM 6361 CD1 LEU D 118 73.527 50.143 28.402 1.000 34.18 ATOM 6362 CD2 LEU D 118 72.426 48.174 27.297 1.000 39.23 ATOM 6363 C LEU D 118 69.018 49.334 29.531 1.000 24.46 ATOM 6364 O LEU D 118 68.965 48.499 30.430 1.000 26.50 ATOM 6365 N ASP D 119 68.433 50.529 29.604 1.000 23.45 ATOM 6366 CA ASP D 119 67.734 50.943 30.813 1.000 20.49 ATOM 6367 CE ASP D 119 67.298 52.402 30.675 1.000 21.70 ATOM 6368 CG ASP D 119 68.469 53.349 30.876 1.000 24.66 ATOM 6369 OD1 ASP D 119 68.249 54.577 30.868 1.000 37.01 ATOM 6370 OD2 ASP D 119 69.614 52.870 31.041 1.000 27.68 ATOM 6371 C ASP D 119 66.559 50.025 31.098 1.000 26.03 ATOM 6372 O ASP D 119 66.410 49.543 32.222 1.000 22.46 ATOM 6373 N VAL D 120 65.718 49.766 30.094 1.000 26.23 ATOM 6374 CA VAL D 120 64.566 48.908 30.351 1.000 22.36 ATOM 6375 CB VAL D 120 63.511 48.983 29.231 1.000 22.81 ATOM 6376 CG1 VAL D 120 62.412 47.954 29.466 1.000 19.93 ATOM 6377 CG2 VAL D 120 62.907 50.375 29.137 1.000 28.30 ATOM 6378 C VAL D 120 64.978 47.450 30.514 1.000 22.74 ATOM 6379 O VAL D 120 64.605 46.804 31.495 1.000 24.55 ATOM 6380 N ASN D 121 65.734 46.919 29.547 1.000 18.38 ATOM 6381 CA ASN D 121 66.020 45.497 29.514 1.000 15.30 ATOM 6382 CB ASN D 121 66.583 45.094 28.143 1.000 20.69 ATOM 6383 CG ASN D 121 65.530 45.119 27.056 1.000 26.58 ATOM 6384 OD1 ASN D 121 64.352 45.388 27.314 1.000 27.53 ATOM 6385 ND2 ASN D 121 65.934 44.844 25.825 1.000 21.69 ATOM 6386 C ASN D 121 67.013 45.050 30.583 1.000 18.37 ATOM 6387 O ASN D 121 66.808 43.983 31.166 1.000 20.46 ATOM 6388 N LEU D 122 68.053 45.842 30.793 1.000 20.17 ATOM 6389 CA LEU D 122 69.172 45.423 31.640 1.000 18.87 ATOM 6390 CB LEU D 122 70.488 45.759 30.940 1.000 20.22 ATOM 6391 CG LEU D 122 71.785 45.431 31.679 1.000 22.50 ATOM 6392 CD1 LEU D 122 71.791 43.969 32.116 1.000 19.47 ATOM 6393 CD2 LEU D 122 73.002 45.739 30.815 1.000 13.29 ATOM 6394 C LEU D 122 69.097 46.064 33.024 1.000 22.74 ATOM 6395 O LEU D 122 69.042 45.339 34.022 1.000 23.12 ATOM 6396 N MET D 123 69.094 47.391 33.110 1.000 19.62 ATOM 6397 CA MET D 123 69.023 48.058 34.414 1.000 21.53 ATOM 6398 CB MET D 123 69.176 49.565 34.258 1.000 24.22 ATOM 6399 CG MET D 123 69.034 50.403 35.516 1.000 25.27 ATOM 6400 SD MET D 123 67.343 50.956 35.801 1.000 26.68 ATOM 6401 CE MET D 123 67.209 52.315 34.650 1.000 23.05 ATOM 6402 C MET D 123 67.712 47.704 35.106 1.000 26.27 ATOM 6403 O MET D 123 67.674 47.364 36.288 1.000 22.41 ATOM 6404 N GLY D 124 66.604 47.765 34.368 1.000 23.16 ATOM 6405 CA GLY D 124 65.306 47.408 34.921 1.000 23.30 ATOM 6406 C GLY D 124 65.311 46.009 35.507 1.000 28.26 ATOM 6407 O GLY D 124 64.760 45.783 36.589 1.000 25.60 ATOM 6408 N THR D 125 65.922 45.053 34.808 1.000 21.28 ATOM 6409 CA THR D 125 65.981 43.687 35.340 1.000 18.79 ATOM 6410 CB THR D 125 66.528 42.692 34.307 1.000 19.73 ATOM 6411 OG1 THR D 125 65.460 42.277 33.438 1.000 20.94 ATOM 6412 CG2 THR D 125 67.039 41.421 34.966 1.000 19.51 ATOM 6413 C THR D 125 66.813 43.663 36.617 1.000 20.50 ATOM 6414 O THR D 125 66.383 43.054 37.602 1.000 22.54 ATOM 6415 N PHE D 126 67.969 44.318 36.623 1.000 22.38 ATOM 6416 CA PHE D 126 68.769 44.394 37.843 1.000 23.35 ATOM 6417 CE PHE D 126 70.122 45.087 37.643 1.000 18.53 ATOM 6418 CG PHE D 126 70.989 45.079 38.896 1.000 25.35 ATOM 6419 CD1 PHE D 126 71.667 43.943 39.293 1.000 24.48 ATOM 6420 CD2 PHE D 126 71.132 46.214 39.680 1.000 29.37 ATOM 6421 CE1 PHE D 126 72.463 43.925 40.430 1.000 21.17 ATOM 6422 CE2 PHE D 126 71.925 46.210 40.819 1.000 27.18 ATOM 6423 CZ PHE D 126 72.606 45.063 41.200 1.000 20.25 ATOM 6424 C PHE D 126 68.004 45.117 38.951 1.000 22.47 ATOM 6425 O PHE D 126 68.123 44.694 40.101 1.000 19.76 ATOM 6426 N ASN D 127 67.248 46.155 38.616 1.000 19.34 ATOM 6427 CA ASN D 127 66.464 46.884 39.614 1.000 23.88 ATOM 6428 CE ASN D 127 65.681 48.036 38.975 1.000 22.44 ATOM 6429 CG ASN D 127 65.039 48.962 39.988 1.000 30.06 ATOM 6430 OD1 ASN D 127 65.566 49.201 41.082 1.000 29.26 ATOM 6431 ND2 ASN D 127 63.878 49.514 39.644 1.000 22.96 ATOM 6432 C ASN D 127 65.518 45.947 40.358 1.000 25.51 ATOM 6433 O ASN D 127 65.516 45.912 41.594 1.000 29.94 ATOM 6434 N VAL D 128 64.727 45.177 39.621 1.000 22.04 ATOM 6435 CA VAL D 128 63.826 44.206 40.243 1.000 24.33 ATOM 6436 CE VAL D 128 62.956 43.507 39.181 1.000 23.82 ATOM 6437 CG1 VAL D 128 62.112 42.395 39.772 1.000 19.10 ATOM 6438 CG2 VAL D 128 62.057 44.530 38.493 1.000 24.29 ATOM 6439 C VAL D 128 64.591 43.173 41.058 1.000 25.09 ATOM 6440 O VAL D 128 64.237 42.900 42.210 1.000 24.73 ATOM 6441 N ILE D 129 65.646 42.588 40.500 1.000 19.60 ATOM 6442 CA ILE D 129 66.413 41.570 41.212 1.000 20.00 ATOM 6443 CB ILE D 129 67.623 41.085 40.386 1.000 19.71 ATOM 6444 CG2 ILE D 129 68.625 40.382 41.290 1.000 20.01 ATOM 6445 CG1 ILE D 129 67.294 40.185 39.197 1.000 20.97 ATOM 6446 CD1 ILE D 129 68.461 40.025 38.231 1.000 20.09 ATOM 6447 C ILE D 129 66.944 42.064 42.555 1.000 22.83 ATOM 6448 O ILE D 129 66.847 41.373 43.577 1.000 23.59 ATOM 6449 N ARG D 130 67.537 43.259 42.570 1.000 21.25 ATOM 6450 CA ARG D 130 68.158 43.727 43.813 1.000 23.54 ATOM 6451 CE ARG D 130 68.999 44.977 43.560 1.000 22.14 ATOM 6452 CG ARG D 130 68.195 46.253 43.482 1.000 20.61 ATOM 6453 CD ARG D 130 68.975 47.455 42.942 1.000 19.85 ATOM 6454 NE ARG D 130 67.980 48.538 42.867 1.000 25.36 ATOM 6455 CZ ARG D 130 67.805 49.473 43.786 1.000 25.50 ATOM 6456 NH1 ARG D 130 66.868 50.401 43.628 1.000 20.78 ATOM 6457 NH2 ARG D 130 68.580 49.482 44.857 1.000 19.51 ATOM 6458 C ARG D 130 67.096 43.971 44.877 1.000 27.48 ATOM 6459 O ARG D 130 67.303 43.695 46.061 1.000 23.84 ATOM 6460 N LEU D 131 65.932 44.474 44.473 1.000 27.06 ATOM 6461 CA LEU D 131 64.884 44.753 45.458 1.000 28.21 ATOM 6462 CB LEU D 131 63.895 45.787 44.910 1.000 23.68 ATOM 6463 CG LEU D 131 64.445 47.216 44.808 1.000 26.52 ATOM 6464 CD1 LEU D 131 63.477 48.145 44.089 1.000 23.04 ATOM 6465 CD2 LEU D 131 64.770 47.782 46.188 1.000 32.33 ATOM 6466 C LEU D 131 64.189 43.471 45.891 1.000 29.02 ATOM 6467 O LEU D 131 63.973 43.244 47.089 1.000 26.84 ATOM 6468 N VAL D 132 63.846 42.601 44.947 1.000 18.42 ATOM 6469 CA VAL D 132 63.159 41.367 45.325 1.000 18.90 ATOM 6470 CB VAL D 132 62.618 40.598 44.106 1.000 23.35 ATOM 6471 CG1 VAL D 132 63.708 39.751 43.463 1.000 23.66 ATOM 6472 CG2 VAL D 132 61.446 39.715 44.506 1.000 22.79 ATOM 6473 C VAL D 132 64.073 40.451 46.132 1.000 23.76 ATOM 6474 O VAL D 132 63.616 39.657 46.953 1.000 27.48 ATOM 6475 N ALA D 133 65.389 40.531 45.932 1.000 22.04 ATOM 6476 CA ALA D 133 66.297 39.729 46.754 1.000 23.76 ATOM 6477 CB ALA D 133 67.730 39.926 46.302 1.000 20.82 ATOM 6478 C ALA D 133 66.148 40.103 48.230 1.000 24.85 ATOM 6479 O ALA D 133 66.290 39.282 49.131 1.000 23.50 ATOM 6480 N GLY D 134 65.852 41.376 48.460 1.000 26.12 ATOM 6481 CA GLY D 134 65.563 41.870 49.793 1.000 32.35 ATOM 6482 C GLY D 134 64.285 41.284 50.357 1.000 34.57 ATOM 6483 O GLY D 134 64.202 41.047 51.568 1.000 35.22 ATOM 6484 N GLU D 135 63.277 41.038 49.523 1.000 30.01 ATOM 6485 CA GLU D 135 62.034 40.496 50.068 1.000 28.91 ATOM 6486 CE GLU D 135 60.839 40.738 49.147 1.000 26.20 ATOM 6487 CG GLU D 135 60.598 42.200 48.824 1.000 30.37 ATOM 6488 CD GLU D 135 60.124 42.990 50.027 1.000 35.33 ATOM 6489 OE1 GLU D 135 60.588 44.135 50.204 1.000 44.37 ATOM 6490 OE2 GLU D 135 59.294 42.447 50.785 1.000 45.78 ATOM 6491 C GLU D 135 62.163 39.001 50.343 1.000 30.94 ATOM 6492 O GLU D 135 61.616 38.487 51.323 1.000 32.39 ATOM 6493 N MET D 136 62.873 38.287 49.475 1.000 23.95 ATOM 6494 CA MET D 136 63.071 36.860 49.680 1.000 23.00 ATOM 6495 CB MET D 136 63.685 36.218 48.428 1.000 27.92 ATOM 6496 CG MET D 136 62.749 36.166 47.227 1.000 30.16 ATOM 6497 SD MET D 136 63.670 35.935 45.689 1.000 23.75 ATOM 6498 CE MET D 136 62.344 35.879 44.489 1.000 20.24 ATOM 6499 C MET D 136 63.986 36.591 50.868 1.000 21.34 ATOM 6500 O MET D 136 63.924 35.549 51.518 1.000 26.69 ATOM 6501 N GLY D 137 64.877 37.539 51.158 1.000 23.58 ATOM 6502 CA GLY D 137 65.799 37.353 52.276 1.000 27.87 ATOM 6503 C GLY D 137 65.026 37.196 53.578 1.000 34.97 ATOM 6504 O GLY D 137 65.484 36.540 54.512 1.000 32.81 ATOM 6505 N GLN D 138 63.837 37.798 53.610 1.000 29.09 ATOM 6506 CA GLN D 138 62.998 37.802 54.802 1.000 30.46 ATOM 6507 CB GLN D 138 61.956 38.908 54.691 1.000 33.07 ATOM 6508 C GLN D 138 62.327 36.459 55.039 1.000 34.33 ATOM 6509 O GLN D 138 61.800 36.204 56.124 1.000 36.30 ATOM 6510 N ASN D 139 62.341 35.587 54.028 1.000 31.51 ATOM 6511 CA ASN D 139 61.696 34.291 54.219 1.000 28.20 ATOM 6512 CB ASN D 139 61.363 33.612 52.900 1.000 27.26 ATOM 6513 CG ASN D 139 60.572 34.464 51.932 1.000 34.45 ATOM 6514 OD1 ASN D 139 59.779 35.315 52.340 1.000 32.80 ATOM 6515 ND2 ASN D 139 60.798 34.227 50.642 1.000 25.07 ATOM 6516 C ASN D 139 62.606 33.367 55.024 1.000 32.92 ATOM 6517 O ASN D 139 63.820 33.396 54.827 1.000 30.48 ATOM 6518 N GLU D 140 62.025 32.552 55.903 1.000 30.73 ATOM 6519 CA GLU D 140 62.828 31.514 56.550 1.000 32.23 ATOM 6520 CE GLU D 140 62.098 30.903 57.730 1.000 38.83 ATOM 6521 C GLU D 140 63.174 30.453 55.510 1.000 32.14 ATOM 6522 O GLU D 140 62.303 30.103 54.706 1.000 31.41 ATOM 6523 N PRO D 141 64.397 29.942 55.494 1.000 30.57 ATOM 6524 CD PRO D 141 65.498 30.258 56.412 1.000 30.81 ATOM 6525 CA PRO D 141 64.771 28.949 54.483 1.000 28.26 ATOM 6526 CB PRO D 141 66.204 28.575 54.847 1.000 32.66 ATOM 6527 CG PRO D 141 66.701 29.650 55.748 1.000 32.60 ATOM 6528 C PRO D 141 63.877 27.717 54.550 1.000 35.61 ATOM 6529 O PRO D 141 63.444 27.315 55.630 1.000 38.04 ATOM 6530 N ASP D 142 63.595 27.116 53.391 1.000 31.00 ATOM 6531 CA ASP D 142 62.833 25.868 53.394 1.000 30.24 ATOM 6532 CB ASP D 142 62.203 25.612 52.035 1.000 35.96 ATOM 6533 CG ASP D 142 63.154 25.321 50.898 1.000 34.68 ATOM 6534 OD1 ASP D 142 64.363 25.098 51.104 1.000 27.65 ATOM 6535 OD2 ASP D 142 62.670 25.303 49.742 1.000 33.75 ATOM 6536 C ASP D 142 63.741 24.710 53.799 1.000 34.08 ATOM 6537 O ASP D 142 64.880 24.929 54.213 1.000 29.73 ATOM 6538 N GLN D 143 63.245 23.487 53.653 1.000 34.49 ATOM 6539 CA GLN D 143 64.011 22.307 54.043 1.000 39.62 ATOM 6540 CB GLN D 143 63.204 21.045 53.757 1.000 38.01 ATOM 6541 C GLN D 143 65.369 22.242 53.346 1.000 41.65 ATOM 6542 O GLN D 143 66.328 21.695 53.900 1.000 35.45 ATOM 6543 N GLY D 144 65.443 22.791 52.136 1.000 37.16 ATOM 6544 CA GLY D 144 66.661 22.736 51.337 1.000 30.96 ATOM 6545 C GLY D 144 67.455 24.022 51.448 1.000 31.88 ATOM 6546 O GLY D 144 68.358 24.282 50.651 1.000 29.80 ATOM 6547 N GLY D 145 67.119 24.841 52.445 1.000 28.25 ATOM 6548 CA GLY D 145 67.786 26.101 52.691 1.000 24.94 ATOM 6549 C GLY D 145 67.436 27.188 51.692 1.000 25.03 ATOM 6550 O GLY D 145 68.057 28.252 51.660 1.000 22.98 ATOM 6551 N GLN D 146 66.438 26.952 50.854 1.000 23.54 ATOM 6552 CA GLN D 146 66.079 27.907 49.818 1.000 25.58 ATOM 6553 CB GLN D 146 65.402 27.173 48.646 1.000 26.63 ATOM 6554 CG GLN D 146 65.240 28.068 47.420 1.000 31.76 ATOM 6555 CD GLN D 146 64.934 27.273 46.163 1.000 30.74 ATOM 6556 OE1 GLN D 146 65.837 26.723 45.538 1.000 26.69 ATOM 6557 NE2 GLN D 146 63.659 27.205 45.802 1.000 26.20 ATOM 6558 C GLN D 146 65.155 29.015 50.305 1.000 27.84 ATOM 6559 O GLN D 146 64.176 28.757 51.009 1.000 29.88 ATOM 6560 N ARG D 147 65.476 30.248 49.918 1.000 21.77 ATOM 6561 CA ARG D 147 64.660 31.403 50.244 1.000 20.05 ATOM 6562 CB ARG D 147 65.524 32.520 50.844 1.000 19.56 ATOM 6563 CG ARG D 147 65.830 32.272 52.325 1.000 20.31 ATOM 6564 CD ARG D 147 66.349 33.569 52.933 1.000 25.52 ATOM 6565 NE ARG D 147 66.652 33.413 54.348 1.000 27.20 ATOM 6566 CZ ARG D 147 67.852 33.105 54.824 1.000 33.45 ATOM 6567 NH1 ARG D 147 68.015 32.991 56.135 1.000 36.21 ATOM 6568 NH2 ARG D 147 68.871 32.911 53.997 1.000 25.45 ATOM 6569 C ARG D 147 63.920 31.950 49.032 1.000 27.39 ATOM 6570 O ARG D 147 62.966 32.713 49.198 1.000 27.36 ATOM 6571 N GLY D 148 64.343 31.588 47.822 1.000 26.76 ATOM 6572 CA GLY D 148 63.609 32.056 46.647 1.000 24.31 ATOM 6573 C GLY D 148 64.307 31.704 45.344 1.000 26.16 ATOM 6574 O GLY D 148 65.459 31.252 45.369 1.000 23.81 ATOM 6575 N VAL D 149 63.606 31.924 44.235 1.000 22.84 ATOM 6576 CA VAL D 149 64.141 31.695 42.891 1.000 22.49 ATOM 6577 CB VAL D 149 63.528 30.432 42.267 1.000 23.53 ATOM 6578 CG1 VAL D 149 64.113 30.124 40.899 1.000 24.88 ATOM 6579 CG2 VAL D 149 63.759 29.246 43.201 1.000 29.26 ATOM 6580 C VAL D 149 63.912 32.905 41.991 1.000 24.44 ATOM 6581 O VAL D 149 62.822 33.468 41.902 1.000 19.35 ATOM 6582 N ILE D 150 64.972 33.336 41.313 1.000 23.79 ATOM 6583 CA ILE D 150 64.904 34.472 40.398 1.000 20.68 ATOM 6584 CB ILE D 150 65.857 35.590 40.835 1.000 23.33 ATOM 6585 CG2 ILE D 150 65.950 36.705 39.800 1.000 23.62 ATOM 6586 CG1 ILE D 150 65.499 36.157 42.217 1.000 22.16 ATOM 6587 CD1 ILE D 150 66.361 37.303 42.679 1.000 22.90 ATOM 6588 C ILE D 150 65.221 34.002 38.978 1.000 23.90 ATOM 6589 O ILE D 150 66.265 33.381 38.752 1.000 24.70 ATOM 6590 N ILE D 151 64.323 34.284 38.042 1.000 19.69 ATOM 6591 CA ILE D 151 64.461 33.829 36.660 1.000 18.08 ATOM 6592 CB ILE D 151 63.373 32.811 36.275 1.000 20.01 ATOM 6593 CG2 ILE D 151 63.556 32.325 34.840 1.000 16.55 ATOM 6594 CG ILE D 151 63.272 31.620 37.227 1.000 21.12 ATOM 6595 CD1 ILE D 151 62.210 30.603 36.855 1.000 22.94 ATOM 6596 C ILE D 151 64.402 35.029 35.721 1.000 23.47 ATOM 6597 O ILE D 151 63.402 35.757 35.733 1.000 23.16 ATOM 6598 N ASN D 152 65.469 35.201 34.939 1.000 22.25 ATOM 6599 CA ASN D 152 65.566 36.340 34.031 1.000 17.00 ATOM 6600 CB ASN D 152 66.939 36.993 34.163 1.000 18.22 ATOM 6601 CG ASN D 152 67.347 37.129 35.623 1.000 22.84 ATOM 6602 OD1 ASN D 152 68.340 36.563 36.091 1.000 31.50 ATOM 6603 ND2 ASN D 152 66.542 37.898 36.341 1.000 16.63 ATOM 6604 C ASN D 152 65.316 35.937 32.581 1.000 20.23 ATOM 6605 O ASN D 152 65.391 34.767 32.229 1.000 21.50 ATOM 6606 N THR D 153 65.014 36.907 31.733 1.000 23.06 ATOM 6607 CA THR D 153 64.800 36.646 30.313 1.000 20.08 ATOM 6608 CB THR D 153 63.407 37.093 29.843 1.000 22.69 ATOM 6609 OG1 THR D 153 62.392 36.524 30.690 1.000 19.08 ATOM 6610 CG2 THR D 153 63.126 36.586 28.434 1.000 22.90 ATOM 6611 C THR D 153 65.868 37.376 29.503 1.000 19.71 ATOM 6612 O THR D 153 65.902 38.606 29.459 1.000 18.87 ATOM 6613 N ALA D 154 66.757 36.605 28.882 1.000 19.04 ATOM 6614 CA ALA D 154 67.764 37.172 27.989 1.000 20.22 ATOM 6615 CB ALA D 154 69.095 36.482 28.191 1.000 14.81 ATOM 6616 C ALA D 154 67.240 37.026 26.557 1.000 21.98 ATOM 6617 O ALA D 154 66.100 37.430 26.300 1.000 20.90 ATOM 6618 N SER D 155 68.029 36.446 25.669 1.000 22.69 ATOM 6619 CA SER D 155 67.658 36.189 24.279 1.000 20.37 ATOM 6620 CE SER D 155 67.301 37.486 23.550 1.000 21.64 ATOM 6621 OG SER D 155 67.329 37.338 22.133 1.000 21.48 ATOM 6622 C SER D 155 68.801 35.494 23.554 1.000 18.34 ATOM 6623 O SER D 155 69.956 35.714 23.932 1.000 19.68 ATOM 6624 N VAL D 156 68.553 34.690 22.514 1.000 15.42 ATOM 6625 CA VAL D 156 69.710 34.158 21.782 1.000 17.65 ATOM 6626 CB VAL D 156 69.313 33.125 20.714 1.000 21.51 ATOM 6627 CG1 VAL D 156 68.671 31.920 21.384 1.000 23.31 ATOM 6628 CG2 VAL D 156 68.391 33.752 19.683 1.000 24.15 ATOM 6629 C VAL D 156 70.522 35.265 21.125 1.000 15.00 ATOM 6630 O VAL D 156 71.678 35.056 20.758 1.000 21.65 ATOM 6631 N ALA D 157 69.976 36.468 20.988 1.000 17.14 ATOM 6632 CA ALA D 157 70.710 37.651 20.578 1.000 17.24 ATOM 6633 CB ALA D 157 69.769 38.855 20.568 1.000 13.94 ATOM 6634 C ALA D 157 71.916 37.921 21.470 1.000 23.46 ATOM 6635 O ALA D 157 72.845 38.627 21.064 1.000 21.41 ATOM 6636 N ALA D 158 71.942 37.380 22.689 1.000 23.28 ATOM 6637 CA ALA D 158 73.113 37.504 23.546 1.000 23.19 ATOM 6638 CE ALA D 158 72.861 36.891 24.918 1.000 18.33 ATOM 6639 C ALA D 158 74.327 36.834 22.904 1.000 20.07 ATOM 6640 O ALA D 158 75.477 37.201 23.164 1.000 18.25 ATOM 6641 N PHE D 159 74.043 35.844 22.068 1.000 16.93 ATOM 6642 CA PHE D 159 75.090 34.998 21.504 1.000 20.37 ATOM 6643 CE PHE D 159 74.764 33.527 21.785 1.000 22.16 ATOM 6644 CG PHE D 159 74.507 33.240 23.261 1.000 23.66 ATOM 6645 CD1 PHE D 159 73.247 32.850 23.687 1.000 24.05 ATOM 6646 CD2 PHE D 159 75.528 33.361 24.184 1.000 21.58 ATOM 6647 CE1 PHE D 159 72.996 32.585 25.025 1.000 21.33 ATOM 6648 CE2 PHE D 159 75.285 33.112 25.522 1.000 26.43 ATOM 6649 CZ PHE D 159 74.024 32.723 25.940 1.000 22.81 ATOM 6650 C PHE D 159 75.301 35.191 20.004 1.000 26.53 ATOM 6651 O PHE D 159 76.448 35.093 19.557 1.000 22.13 ATOM 6652 N GLU D 160 74.247 35.455 19.235 1.000 22.81 ATOM 6653 CA GLU D 160 74.367 35.655 17.797 1.000 25.82 ATOM 6654 CB GLU D 160 73.868 34.471 16.977 1.000 26.92 ATOM 6655 CG GLU D 160 74.398 33.097 17.272 1.000 31.97 ATOM 6656 CD GLU D 160 73.390 32.186 17.945 1.000 33.94 ATOM 6657 OE1 GLU D 160 73.834 31.464 18.863 1.000 27.97 ATOM 6658 OE2 GLU D 160 72.188 32.168 17.592 1.000 26.48 ATOM 6659 C GLU D 160 73.553 36.876 17.356 1.000 21.87 ATOM 6660 O GLU D 160 72.678 36.727 16.497 1.000 19.91 ATOM 6661 N GLY D 161 73.821 38.038 17.936 1.000 18.43 ATOM 6662 CA GLY D 161 73.065 39.235 17.596 1.000 18.74 ATOM 6663 C GLY D 161 73.061 39.461 16.090 1.000 23.77 ATOM 6664 O GLY D 161 74.125 39.344 15.479 1.000 20.48 ATOM 6665 N GLN D 162 71.900 39.766 15.529 1.000 20.27 ATOM 6666 CA GLN D 162 71.720 39.960 14.104 1.000 23.42 ATOM 6667 CB GLN D 162 70.259 39.671 13.743 1.000 21.25 ATOM 6668 CG GLN D 162 69.841 38.219 13.946 1.000 23.82 ATOM 6669 CD GLN D 162 68.525 37.938 13.233 1.000 27.75 ATOM 6670 OE1 GLN D 162 67.457 38.360 13.678 1.000 28.35 ATOM 6671 NE2 GLN D 162 68.613 37.233 12.110 1.000 23.89 ATOM 6672 C GLN D 162 72.061 41.373 13.650 1.000 27.25 ATOM 6673 O GLN D 162 72.231 42.269 14.481 1.000 19.80 ATOM 6674 N VAL D 163 72.134 41.570 12.323 1.000 21.48 ATOM 6675 CA VAL D 163 72.258 42.948 11.835 1.000 19.83 ATOM 6676 CB VAL D 163 72.277 43.041 10.302 1.000 20.25 ATOM 6677 CG1 VAL D 163 72.244 44.493 9.853 1.000 20.85 ATOM 6678 CG2 VAL D 163 73.516 42.368 9.723 1.000 13.02 ATOM 6679 C VAL D 163 71.087 43.765 12.382 1.000 22.78 ATOM 6680 O VAL D 163 69.938 43.310 12.304 1.000 26.26 ATOM 6681 N GLY D 164 71.354 44.932 12.951 1.000 21.30 ATOM 6682 CA GLY D 164 70.329 45.774 13.539 1.000 20.37 ATOM 6683 C GLY D 164 70.094 45.539 15.021 1.000 22.49 ATOM 6684 O GLY D 164 69.353 46.305 15.649 1.000 24.72 ATOM 6685 N GLN D 165 70.695 44.515 15.613 1.000 23.42 ATOM 6686 CA GLN D 165 70.439 44.131 16.990 1.000 23.82 ATOM 6687 CB GLN D 165 70.290 42.598 17.070 1.000 22.26 ATOM 6688 CG GLN D 165 68.949 42.087 16.586 1.000 27.27 ATOM 6689 CD GLN D 165 68.682 40.656 16.998 1.000 27.39 ATOM 6690 OE1 GLN D 165 69.560 39.798 16.983 1.000 23.93 ATOM 6691 NE2 GLN D 165 67.434 40.395 17.379 1.000 30.12 ATOM 6692 C GLN D 165 71.506 44.522 18.001 1.000 23.76 ATOM 6693 O GLN D 165 71.501 43.947 19.103 1.000 24.07 ATOM 6694 N ALA D 166 72.408 45.444 17.708 1.000 17.21 ATOM 6695 CA ALA D 166 73.443 45.806 18.674 1.000 19.58 ATOM 6696 CB ALA D 166 74.299 46.938 18.104 1.000 21.71 ATOM 6697 C ALA D 166 72.925 46.236 20.043 1.000 21.41 ATOM 6698 O ALA D 166 73.392 45.739 21.072 1.000 21.84 ATOM 6699 N ALA D 167 71.987 47.182 20.137 1.000 19.77 ATOM 6700 CA ALA D 167 71.574 47.641 21.470 1.000 20.56 ATOM 6701 CB ALA D 167 70.649 48.841 21.357 1.000 19.93 ATOM 6702 C ALA D 167 70.916 46.514 22.258 1.000 23.33 ATOM 6703 O ALA D 167 71.250 46.237 23.410 1.000 23.45 ATOM 6704 N TYR D 168 69.963 45.845 21.612 1.000 21.23 ATOM 6705 CA TYR D 168 69.279 44.702 22.199 1.000 18.68 ATOM 6706 CE TYR D 168 68.301 44.123 21.175 1.000 19.46 ATOM 6707 CG TYR D 168 67.308 43.119 21.706 1.000 17.17 ATOM 6708 CD1 TYR D 168 66.289 43.509 22.577 1.000 20.81 ATOM 6709 CE1 TYR D 168 65.389 42.575 23.056 1.000 17.29 ATOM 6710 CD2 TYR D 168 67.393 41.785 21.336 1.000 14.49 ATOM 6711 CE2 TYR D 168 66.496 40.846 21.809 1.000 18.56 ATOM 6712 CZ TYR D 168 65.494 41.263 22.672 1.000 22.02 ATOM 6713 OH TYR D 168 64.599 40.334 23.142 1.000 21.10 ATOM 6714 C TYR D 168 70.264 43.634 22.647 1.000 22.16 ATOM 6715 O TYR D 168 70.176 43.093 23.750 1.000 22.67 ATOM 6716 N SER D 169 71.222 43.314 21.778 1.000 19.55 ATOM 6717 CA SER D 169 72.216 42.298 22.096 1.000 17.20 ATOM 6718 CE SER D 169 73.152 42.059 20.915 1.000 18.47 ATOM 6719 OG SER D 169 72.489 41.424 19.838 1.000 21.29 ATOM 6720 C SER D 169 73.023 42.705 23.328 1.000 20.02 ATOM 6721 O SER D 169 73.348 41.871 24.172 1.000 24.34 ATOM 6722 N ALA D 170 73.343 43.985 23.419 1.000 20.02 ATOM 6723 CA ALA D 170 74.107 44.518 24.540 1.000 17.28 ATOM 6724 CB ALA D 170 74.415 45.986 24.317 1.000 16.21 ATOM 6725 C ALA D 170 73.324 44.324 25.834 1.000 22.82 ATOM 6726 O ALA D 170 73.862 43.921 26.866 1.000 21.81 ATOM 6727 N SER D 171 72.027 44.617 25.765 1.000 19.01 ATOM 6728 CA SER D 171 71.196 44.486 26.965 1.000 20.11 ATOM 6729 CE SER D 171 69.838 45.160 26.723 1.000 18.33 ATOM 6730 OG SER D 171 68.954 44.319 26.011 1.000 16.83 ATOM 6731 C SER D 171 71.042 43.034 27.378 1.000 18.43 ATOM 6732 O SER D 171 71.058 42.715 28.571 1.000 25.54 ATOM 6733 N LYS D 172 70.894 42.104 26.438 1.000 16.24 ATOM 6734 CA LYS D 172 70.682 40.710 26.836 1.000 18.91 ATOM 6735 CB LYS D 172 69.934 39.934 25.747 1.000 18.86 ATOM 6736 CG LYS D 172 68.587 40.565 25.386 1.000 18.26 ATOM 6737 CD LYS D 172 67.692 40.665 26.608 1.000 22.32 ATOM 6738 CE LYS D 172 66.249 40.992 26.239 1.000 20.18 ATOM 6739 NZ LYS D 172 65.329 40.645 27.368 1.000 15.72 ATOM 6740 C LYS D 172 72.001 40.028 27.183 1.000 22.11 ATOM 6741 O LYS D 172 72.064 39.103 27.992 1.000 18.61 ATOM 6742 N GLY D 173 73.093 40.486 26.578 1.000 22.19 ATOM 6743 CA GLY D 173 74.416 39.982 26.932 1.000 21.20 ATOM 6744 C GLY D 173 74.755 40.367 28.368 1.000 24.62 ATOM 6745 O GLY D 173 75.413 39.611 29.088 1.000 19.92 ATOM 6746 N GLY D 174 74.290 41.550 28.754 1.000 18.59 ATOM 6747 CA GLY D 174 74.439 42.031 30.122 1.000 20.37 ATOM 6748 C GLY D 174 73.709 41.098 31.069 1.000 18.89 ATOM 6749 O GLY D 174 74.213 40.687 32.107 1.000 18.97 ATOM 6750 N ILE D 175 72.486 40.722 30.700 1.000 20.45 ATOM 6751 CA ILE D 175 71.723 39.800 31.524 1.000 17.82 ATOM 6752 CB ILE D 175 70.355 39.443 30.914 1.000 20.89 ATOM 6753 CG2 ILE D 175 69.652 38.433 31.819 1.000 20.20 ATOM 6754 CD1 ILE D 175 69.440 40.623 30.598 1.000 23.10 ATOM 6755 CD1 ILE D 175 68.826 41.265 31.823 1.000 32.75 ATOM 6756 C ILE D 175 72.507 38.502 31.715 1.000 21.19 ATOM 6757 O ILE D 175 72.707 38.002 32.820 1.000 19.56 ATOM 6758 N VAL D 176 72.955 37.955 30.580 1.000 14.04 ATOM 6759 CA VAL D 176 73.713 36.712 30.628 1.000 11.58 ATOM 6760 CB VAL D 176 74.130 36.242 29.227 1.000 17.57 ATOM 6761 CD1 VAL D 176 75.234 35.197 29.299 1.000 17.28 ATOM 6762 CG2 VAL D 176 72.935 35.658 28.488 1.000 17.75 ATOM 6763 C VAL D 176 74.926 36.885 31.530 1.000 17.55 ATOM 6764 O VAL D 176 75.165 36.092 32.446 1.000 21.64 ATOM 6765 N GLY D 177 75.699 37.937 31.293 1.000 18.96 ATOM 6766 CA GLY D 177 76.901 38.179 32.074 1.000 22.45 ATOM 6767 C GLY D 177 76.665 38.201 33.569 1.000 23.71 ATOM 6768 O GLY D 177 77.389 37.578 34.353 1.000 23.04 ATOM 6769 N MET D 178 75.642 38.921 34.024 1.000 20.74 ATOM 6770 CA MET D 178 75.510 39.100 35.474 1.000 16.25 ATOM 6771 CB MET D 178 74.805 40.429 35.761 1.000 17.85 ATOM 6772 CG MET D 178 73.310 40.419 35.552 1.000 20.61 ATOM 6773 SD MET D 178 72.557 42.064 35.615 1.000 22.26 ATOM 6774 CE MET D 178 70.829 41.601 35.430 1.000 20.09 ATOM 6775 C MET D 178 74.798 37.935 36.138 1.000 21.07 ATOM 6776 O MET D 178 74.650 37.936 37.365 1.000 26.74 ATOM 6777 N THR D 179 74.365 36.937 35.377 1.000 17.91 ATOM 6778 CA THR D 179 73.662 35.794 35.963 1.000 17.03 ATOM 6779 CE THR D 179 73.222 34.809 34.867 1.000 17.80 ATOM 6780 OG1 THR D 179 72.125 35.389 34.132 1.000 20.57 ATOM 6781 CG2 THR D 179 72.653 33.530 35.435 1.000 13.48 ATOM 6782 C THR D 179 74.503 35.081 37.016 1.000 24.62 ATOM 6783 O THR D 179 74.029 34.783 38.118 1.000 19.91 ATOM 6784 N LEU D 180 75.766 34.780 36.726 1.000 22.11 ATOM 6785 CA LEU D 180 76.579 34.011 37.660 1.000 20.85 ATOM 6786 CB LEU D 180 77.853 33.468 37.000 1.000 17.23 ATOM 6787 CG LEU D 180 78.726 32.563 37.868 1.000 23.31 ATOM 6788 CD1 LEU D 180 77.953 31.346 38.359 1.000 24.22 ATOM 6789 CD2 LEU D 180 79.961 32.102 37.105 1.000 20.74 ATOM 6790 C LEU D 180 76.966 34.827 38.885 1.000 17.46 ATOM 6791 O LEU D 180 76.746 34.341 40.005 1.000 22.39 ATOM 6792 N PRO D 181 77.537 36.015 38.738 1.000 20.05 ATOM 6793 CD PRO D 181 77.909 36.728 37.503 1.000 20.38 ATOM 6794 CA PRO D 181 77.888 36.811 39.924 1.000 19.83 ATOM 6795 CE PRO D 181 78.326 38.161 39.362 1.000 21.03 ATOM 6796 CG PRO D 181 77.874 38.169 37.937 1.000 18.92 ATOM 6797 C PRO D 181 76.689 37.006 40.852 1.000 27.11 ATOM 6798 O PRO D 181 76.820 36.935 42.073 1.000 21.78 ATOM 6799 N ILE D 182 75.503 37.244 40.292 1.000 19.37 ATOM 6800 CA ILE D 182 74.352 37.452 41.183 1.000 21.03 ATOM 6801 CB ILE D 182 73.147 38.033 40.425 1.000 21.11 ATOM 6802 CG2 ILE D 182 71.913 38.080 41.319 1.000 21.57 ATOM 6803 CG1 ILE D 182 73.455 39.408 39.820 1.000 16.88 ATOM 6804 CD1 ILE D 182 72.306 40.003 39.025 1.000 17.64 ATOM 6805 C ILE D 182 74.017 36.152 41.893 1.000 23.82 ATOM 6806 O ILE D 182 73.800 36.167 43.107 1.000 26.22 ATOM 6807 N ALA D 183 74.005 35.031 41.184 1.000 17.60 ATOM 6808 CA ALA D 183 73.869 33.728 41.811 1.000 19.31 ATOM 6809 CE ALA D 183 74.016 32.621 40.773 1.000 21.49 ATOM 6810 C ALA D 183 74.896 33.551 42.927 1.000 26.28 ATOM 6811 O ALA D 183 74.589 33.085 44.030 1.000 23.11 ATOM 6812 N ARG D 184 76.151 33.915 42.660 1.000 22.78 ATOM 6813 CA ARG D 184 77.187 33.722 43.684 1.000 22.18 ATOM 6814 CE ARG D 184 78.580 33.916 43.085 1.000 18.95 ATOM 6815 CG ARG D 184 78.931 32.878 42.009 1.000 17.71 ATOM 6816 CD ARG D 184 80.151 33.303 41.199 1.000 17.27 ATOM 6817 NE ARG D 184 80.957 32.169 40.756 1.000 22.17 ATOM 6818 CZ ARG D 184 82.097 32.262 40.075 1.000 20.70 ATOM 6819 NE1 ARG D 184 82.769 31.175 39.713 1.000 18.72 ATOM 6820 NH2 ARG D 184 82.604 33.433 39.729 1.000 20.42 ATOM 6821 C ARG D 184 76.928 34.665 44.856 1.000 21.95 ATOM 6822 O ARG D 184 77.117 34.326 46.023 1.000 20.58 ATOM 6823 N ASP D 185 76.481 35.880 44.553 1.000 17.40 ATOM 6824 CA ASP D 185 76.133 36.868 45.5S9 1.000 21.73 ATOM 6825 CE ASP D 185 75.556 38.119 44.889 1.000 23.14 ATOM 6826 CG ASP D 185 76.585 39.134 44.439 1.000 24.36 ATOM 6827 OD1 ASP D 185 76.175 40.163 43.853 1.000 18.99 ATOM 6828 OD2 ASP D 185 77.797 38.915 44.663 1.000 18.75 ATOM 6829 C ASP D 185 75.106 36.341 46.558 1.000 24.87 ATOM 6830 O ASP D 185 75.252 36.478 47.770 1.000 21.06 ATOM 6831 N LEU D 186 74.045 35.743 46.034 1.000 19.83 ATOM 6832 CA LEU D 186 72.899 35.313 46.806 1.000 19.79 ATOM 6833 CB LEU D 186 71.614 35.532 45.994 1.000 20.78 ATOM 6834 CG LEU D 186 71.429 36.936 45.408 1.000 20.00 ATOM 6835 CD1 LEU D 186 70.170 37.010 44.564 1.000 19.62 ATOM 6836 CD2 LEU D 186 71.393 37.976 46.520 1.000 19.25 ATOM 6837 C LEU D 186 73.005 33.854 47.219 1.000 22.76 ATOM 6838 O LEU D 186 72.143 33.371 47.959 1.000 23.72 ATOM 6839 N ALA D 187 74.028 33.132 46.764 1.000 15.74 ATOM 6840 CA ALA D 187 74.188 31.740 47.180 1.000 17.58 ATOM 6841 CB ALA D 187 75.487 31.143 46.634 1.000 15.12 ATOM 6842 C ALA D 187 74.159 31.552 48.696 1.000 23.20 ATOM 6843 O ALA D 187 73.479 30.621 49.150 1.000 21.94 ATOM 6844 N PRO D 188 74.875 32.326 49.499 1.000 29.64 ATOM 6845 CD PRO D 188 75.803 33.421 49.152 1.000 28.61 ATOM 6846 CA PRO D 188 74.830 32.099 50.954 1.000 30.11 ATOM 6847 CB PRO D 188 75.861 33.088 51.519 1.000 29.57 ATOM 6848 CG PRO D 188 76.705 33.486 50.354 1.000 33.79 ATOM 6849 C PRO D 188 73.473 32.383 51.576 1.000 32.97 ATOM 6850 O PRO D 188 73.255 32.077 52.759 1.000 31.98 ATOM 6851 N ILE D 189 72.517 32.962 50.845 1.000 29.31 ATOM 6852 CA ILE D 189 71.210 33.125 51.505 1.000 26.68 ATOM 6853 CB ILE D 189 70.758 34.590 51.557 1.000 30.84 ATOM 6854 CG2 ILE D 189 71.669 35.406 52.466 1.000 35.78 ATOM 6855 CG1 ILE D 189 70.637 35.290 50.199 1.000 24.66 ATOM 6856 CD1 ILE D 189 70.003 36.662 50.353 1.000 27.16 ATOM 6857 C ILE D 189 70.141 32.266 50.844 1.000 23.68 ATOM 6858 O ILE D 189 68.958 32.358 51.180 1.000 25.41 ATOM 6859 N GLY D 190 70.549 31.397 49.922 1.000 19.61 ATOM 6860 CA GLY D 190 69.627 30.428 49.369 1.000 20.36 ATOM 6861 C GLY D 190 68.728 30.959 48.283 1.000 23.23 ATOM 6862 O GLY D 190 67.612 30.458 48.095 1.000 25.02 ATOM 6863 N ILE D 191 69.182 31.962 47.526 1.000 17.82 ATOM 6864 CA ILE D 191 68.337 32.406 46.411 1.000 20.45 ATOM 6865 CB ILE D 191 68.109 33.923 46.468 1.000 20.65 ATOM 6866 CG2 ILE D 191 67.353 34.418 45.249 1.000 21.25 ATOM 6867 CD1 ILE D 191 67.405 34.371 47.764 1.000 20.50 ATOM 6868 CD1 ILE D 191 67.413 35.881 47.921 1.000 22.01 ATOM 6869 C ILE D 191 68.967 31.985 45.089 1.000 23.63 ATOM 6870 O ILE D 191 70.081 32.408 44.781 1.000 23.08 ATOM 6871 N ARG D 192 68.262 31.147 44.326 1.000 20.80 ATOM 6872 CA ARG D 192 68.796 30.736 43.025 1.000 18.93 ATOM 6873 CB ARG D 192 68.201 29.418 42.545 1.000 18.33 ATOM 6874 CG ARG D 192 68.551 28.224 43.416 1.000 22.10 ATOM 6875 CD ARG D 192 68.122 26.915 42.778 1.000 21.75 ATOM 6876 NE ARG D 192 66.697 26.654 42.903 1.000 17.92 ATOM 6877 CZ ARG D 192 65.845 26.507 41.903 1.000 22.86 ATOM 6878 NH1 ARG D 192 66.271 26.602 40.645 1.000 20.64 ATOM 6879 NH2 ARG D 192 64.562 26.265 42.159 1.000 21.71 ATOM 6880 C ARG D 192 68.527 31.823 41.989 1.000 20.00 ATOM 6881 O ARG D 192 67.505 32.498 42.062 1.000 18.87 ATOM 6882 N VAL D 193 69.451 31.960 41.050 1.000 23.51 ATOM 6883 CA VAL D 193 69.317 32.881 39.924 1.000 20.41 ATOM 6884 CB VAL D 193 70.296 34.057 39.981 1.000 18.86 ATOM 6885 CG1 VAL D 193 69.897 35.108 38.951 1.000 21.21 ATOM 6886 CG2 VAL D 193 70.350 34.707 41.353 1.000 18.23 ATOM 6887 C VAL D 193 69.512 32.096 38.623 1.000 20.97 ATOM 6888 O VAL D 193 70.555 31.457 38.454 1.000 17.73 ATOM 6889 N MET D 194 68.513 32.133 37.756 1.000 20.64 ATOM 6890 CA MET D 194 68.529 31.440 36.476 1.000 22.07 ATOM 6891 CE MET D 194 67.648 30.190 36.500 1.000 21.33 ATOM 6892 CG MET D 194 68.224 29.017 37.281 1.000 20.38 ATOM 6893 SD MET D 194 69.616 28.228 36.442 1.000 20.76 ATOM 6894 CE MET D 194 68.837 27.768 34.884 1.000 17.01 ATOM 6895 C MET D 194 68.073 32.356 35.339 1.000 27.30 ATOM 6896 O MET D 194 67.397 33.367 35.539 1.000 21.16 ATOM 6897 N THR D 195 68.455 31.985 34.114 1.000 23.91 ATOM 6898 CA THR D 195 68.128 32.823 32.962 1.000 20.67 ATOM 6899 CB THR D 195 69.312 33.716 32.570 1.000 18.13 ATOM 6900 OG1 THR D 195 69.548 34.706 33.575 1.000 19.08 ATOM 6901 CG2 THR D 195 68.991 34.480 31.288 1.000 22.37 ATOM 6902 C THR D 195 67.724 31.964 31.771 1.000 18.10 ATOM 6903 O THR D 195 68.327 30.934 31.484 1.000 22.46 ATOM 6904 N ILE D 196 66.684 32.390 31.071 1.000 18.33 ATOM 6905 CA ILE D 196 66.212 31.696 29.883 1.000 20.86 ATOM 6906 CE ILE D 196 64.703 31.394 29.937 1.000 22.77 ATOM 6907 CG2 ILE D 196 64.239 30.731 28.643 1.000 14.26 ATOM 6908 CG1 ILE D 196 64.281 30.579 31.162 1.000 18.84 ATOM 6909 CD1 ILE D 196 62.793 30.588 31.442 1.000 22.27 ATOM 6910 C ILE D 196 66.532 32.575 28.673 1.000 20.83 ATOM 6911 O ILE D 196 66.290 33.784 28.750 1.000 20.98 ATOM 6912 N ALA D 197 67.078 31.999 27.608 1.000 17.54 ATOM 6913 CA ALA D 197 67.345 32.773 26.391 1.000 20.67 ATOM 6914 CE ALA D 197 68.792 32.645 25.951 1.000 13.19 ATOM 6915 C ALA D 197 66.403 32.309 25.282 1.000 17.72 ATOM 6916 O ALA D 197 66.687 31.344 24.578 1.000 18.42 ATOM 6917 N PRO D 198 65.261 32.961 25.124 1.000 17.47 ATOM 6918 CD PRO D 198 64.771 34.152 25.846 1.000 15.15 ATOM 6919 CA PRO D 198 64.300 32.495 24.121 1.000 17.20 ATOM 6920 CE PRO D 198 63.032 33.292 24.430 1.000 17.15 ATOM 6921 CG PRO D 198 63.273 33.967 25.750 1.000 17.24 ATOM 6922 C PRO D 198 64.791 32.817 22.712 1.000 22.31 ATOM 6923 O PRO D 198 65.467 33.829 22.497 1.000 19.83 ATOM 6924 N GLY D 199 64.436 31.965 21.749 1.000 17.55 ATOM 6925 CA GLY D 199 64.755 32.287 20.357 1.000 21.07 ATOM 6926 C GLY D 199 63.681 33.220 19.807 1.000 24.15 ATOM 6927 O GLY D 199 63.736 34.427 20.012 1.000 27.73 ATOM 6928 N LEU D 200 62.713 32.635 19.118 1.000 24.38 ATOM 6929 CA LEU D 200 61.623 33.365 18.488 1.000 24.40 ATOM 6930 CE LEU D 200 61.721 33.221 16.967 1.000 28.91 ATOM 6931 CG LEU D 200 63.108 33.444 16.346 1.000 27.16 ATOM 6932 CD1 LEU D 200 63.130 32.970 14.899 1.000 24.33 ATOM 6933 CD2 LEU D 200 63.516 34.904 16.436 1.000 25.63 ATOM 6934 C LEU D 200 60.277 32.847 18.981 1.000 18.97 ATOM 6935 O LEU D 200 60.000 31.656 18.864 1.000 22.53 ATOM 6936 N PHE D 201 59.451 33.728 19.530 1.000 18.45 ATOM 6937 CA PHE D 201 58.189 33.308 20.124 1.000 22.22 ATOM 6938 CE PHE D 201 58.225 33.382 21.657 1.000 17.08 ATOM 6939 CG PHE D 201 58.836 32.160 22.310 1.000 21.74 ATOM 6940 CD1 PHE D 201 60.205 31.942 22.252 1.000 19.60 ATOM 6941 CD2 PHE D 201 58.040 31.245 22.973 1.000 22.47 ATOM 6942 CE1 PHE D 201 60.756 30.818 22.845 1.000 18.88 ATOM 6943 CE2 PHE D 201 58.586 30.117 23.556 1.000 23.20 ATOM 6944 CZ PHE D 201 59.952 29.898 23.490 1.000 18.53 ATOM 6945 C PHE D 201 57.036 34.178 19.635 1.000 23.36 ATOM 6946 O PHE D 201 57.182 35.383 19.451 1.000 24.36 ATOM 6947 N GLY D 202 55.883 33.547 19.455 1.000 26.66 ATOM 6948 CA GLY D 202 54.685 34.243 19.015 1.000 29.50 ATOM 6949 C GLY D 202 54.093 35.130 20.095 1.000 28.23 ATOM 6950 O GLY D 202 53.208 34.713 20.838 1.000 32.75 ATOM 6951 N THR D 203 54.592 36.358 20.189 1.000 26.75 ATOM 6952 CA THR D 203 54.092 37.329 21.155 1.000 26.92 ATOM 6953 CB THR D 203 55.088 37.519 22.314 1.000 27.56 ATOM 6954 OG1 THR D 203 56.204 38.265 21.819 1.000 25.50 ATOM 6955 CG2 THR D 203 55.616 36.186 22.821 1.000 27.78 ATOM 6956 C THR D 203 53.858 38.666 20.461 1.000 29.42 ATOM 6957 O THR D 203 54.258 38.806 19.297 1.000 24.92 ATOM 6958 N PRO D 204 53.218 39.635 21.103 1.000 27.18 ATOM 6959 CD PRO D 204 52.478 39.519 22.386 1.000 31.23 ATOM 6960 CA PRO D 204 53.106 40.986 20.553 1.000 28.92 ATOM 6961 CB PRO D 204 52.302 41.731 21.634 1.000 28.70 ATOM 6962 CG PRO D 204 51.473 40.641 22.248 1.000 28.07 ATOM 6963 C PRO D 204 54.434 41.703 20.347 1.000 34.10 ATOM 6964 O PRO D 204 54.463 42.748 19.681 1.000 27.57 ATOM 6965 N LEU D 205 55.538 41.207 20.886 1.000 36.63 ATOM 6966 CA LEU D 205 56.839 41.839 20.646 1.000 31.29 ATOM 6967 CB LEU D 205 57.970 41.039 21.289 1.000 25.52 ATOM 6968 CG LEU D 205 59.327 41.738 21.381 1.000 33.83 ATOM 6969 CD1 LEU D 205 59.273 42.904 22.357 1.000 31.80 ATOM 6970 CD2 LEU D 205 60.421 40.756 21.777 1.000 30.03 ATOM 6971 C LEU D 205 57.101 41.988 19.140 1.000 27.67 ATOM 6972 O LEU D 205 57.624 43.019 18.719 1.000 29.68 ATOM 6973 N LEU D 206 56.733 40.950 18.405 1.000 22.15 ATOM 6974 CA LEU D 206 56.956 40.766 16.983 1.000 35.07 ATOM 6975 CB LEU D 206 57.054 39.268 16.650 1.000 30.73 ATOM 6976 CG LEU D 206 58.128 38.495 17.421 1.000 32.57 ATOM 6977 CD1 LEU D 206 58.364 37.143 16.772 1.000 23.12 ATOM 6978 CD2 LEU D 206 59.406 39.318 17.516 1.000 28.08 ATOM 6979 C LEU D 206 55.868 41.380 16.110 1.000 38.19 ATOM 6980 O LEU D 206 55.972 41.388 14.881 1.000 44.19 ATOM 6981 N THR D 207 54.818 41.901 16.733 1.000 35.74 ATOM 6982 CA THR D 207 53.710 42.454 15.950 1.000 36.62 ATOM 6983 CB THR D 207 52.642 42.991 16.923 1.000 42.60 ATOM 6984 OG1 THR D 207 51.904 41.854 17.406 1.000 42.42 ATOM 6985 CG2 THR D 207 51.661 43.916 16.235 1.000 51.83 ATOM 6986 C THR D 207 54.164 43.523 14.976 1.000 37.29 ATOM 6987 O THR D 207 53.783 43.529 13.800 1.000 36.09 ATOM 6988 N SER D 208 55.003 44.456 15.420 1.000 37.42 ATOM 6989 CA SER D 208 55.423 45.544 14.547 1.000 36.45 ATOM 6990 CB SER D 208 56.185 46.605 15.354 1.000 35.67 ATOM 6991 OG SER D 208 57.285 46.018 16.032 1.000 47.68 ATOM 6992 CB SER D 208 56.301 45.092 13.389 1.000 42.44 ATOM 6993 O SER D 208 56.751 45.943 12.609 1.000 62.16 ATOM 6994 N LEU D 209 56.581 43.800 13.229 1.000 31.60 ATOM 6995 CA LEU D 209 57.357 43.396 12.058 1.000 32.92 ATOM 6996 CB LEU D 209 58.180 42.136 12.299 1.000 35.21 ATOM 6997 CG LEU D 209 59.199 42.141 13.437 1.000 37.69 ATOM 6998 CD1 LEU D 209 59.658 40.717 13.734 1.000 26.82 ATOM 6999 CD2 LEU D 209 60.373 43.050 13.107 1.000 40.66 ATOM 7000 C LEU D 209 56.412 43.134 10.888 1.000 40.62 ATOM 7001 O LEU D 209 55.250 42.782 11.113 1.000 53.21 ATOM 7002 N PRO D 210 56.905 43.287 9.666 1.000 40.78 ATOM 7003 CD PRO D 210 58.218 43.811 9.264 1.000 44.53 ATOM 7004 CA PRO D 210 56.087 42.897 8.513 1.000 33.12 ATOM 7005 CB PRO D 210 56.967 43.192 7.308 1.000 39.69 ATOM 7006 CG PRO D 210 58.040 44.099 7.801 1.000 44.13 ATOM 7007 C PRO D 210 55.796 41.405 8.614 1.000 36.19 ATOM 7008 O PRO D 210 56.693 40.624 8.946 1.000 42.06 ATOM 7009 N GLU D 211 54.557 41.025 8.332 1.000 38.31 ATOM 7010 CA GLU D 211 54.148 39.627 8.332 1.000 37.48 ATOM 7011 CE GLU D 211 52.757 39.506 7.704 1.000 39.60 ATOM 7012 CG GLU D 211 52.665 38.453 6.614 1.000 49.11 ATOM 7013 CD GLU D 211 52.074 37.151 7.118 1.000 61.74 ATOM 7014 OE1 GLU D 211 51.238 36.564 6.399 1.000 74.58 ATOM 7015 OE2 GLU D 211 52.450 36.715 8.230 1.000 74.33 ATOM 7016 C GLU D 211 55.138 38.739 7.586 1.000 42.31 ATOM 7017 O GLU D 211 55.365 37.585 7.954 1.000 36.56 ATOM 7018 N LYS D 212 55.738 39.262 6.519 1.000 45.52 ATOM 7019 CA LYS D 212 56.702 38.481 5.748 1.000 50.03 ATOM 7020 CE LYS D 212 57.078 39.216 4.469 1.000 48.73 ATOM 7021 C LYS D 212 57.937 38.146 6.580 1.000 45.32 ATOM 7022 O LYS D 212 58.293 36.969 6.677 1.000 61.00 ATOM 7023 N VAL D 213 58.583 39.142 7.177 1.000 37.48 ATOM 7024 CA VAL D 213 59.729 38.909 8.051 1.000 40.78 ATOM 7025 CE VAL D 213 60.171 40.192 8.779 1.000 39.38 ATOM 7026 CG1 VAL D 213 61.448 39.944 9.570 1.000 46.30 ATOM 7027 CG2 VAL D 213 60.376 41.330 7.794 1.000 31.44 ATOM 7028 C VAL D 213 59.407 37.836 9.091 1.000 42.11 ATOM 7029 O VAL D 213 60.143 36.868 9.280 1.000 39.28 ATOM 7030 N ARG D 214 58.272 38.029 9.760 1.000 43.00 ATOM 7031 CA ARG D 214 57.786 37.063 10.736 1.000 46.17 ATOM 7032 CE ARG D 214 56.400 37.494 11.234 1.000 50.42 ATOM 7033 CG ARG D 214 56.061 36.950 12.611 1.000 56.83 ATOM 7034 CD ARG D 214 55.009 37.791 13.317 1.000 65.91 ATOM 7035 NE ARG D 214 53.760 37.850 12.561 1.000 69.02 ATOM 7036 CZ ARG D 214 53.306 38.955 11.979 1.000 65.60 ATOM 7037 NE1 ARG D 214 54.004 40.080 12.073 1.000 45.07 ATOM 7038 NE2 ARG D 214 52.163 38.933 11.308 1.000 67.95 ATOM 7039 C ARG D 214 57.728 35.645 10.179 1.000 41.11 ATOM 7040 O ARG D 214 58.314 34.726 10.761 1.000 35.07 ATOM 7041 N ASN D 215 57.034 35.415 9.062 1.000 30.80 ATOM 7042 CA ASN D 215 56.975 34.059 8.515 1.000 31.83 ATOM 7043 CE ASN D 215 56.004 33.938 7.338 1.000 37.92 ATOM 7044 CG ASN D 215 54.623 34.458 7.692 1.000 43.95 ATOM 7045 OD1 ASN D 215 54.286 34.601 8.868 1.000 50.88 ATOM 7046 ND2 ASN D 215 53.821 34.753 6.678 1.000 41.53 ATOM 7047 C ASN D 215 58.356 33.591 8.078 1.000 26.95 ATOM 7048 O ASN D 215 58.701 32.421 8.239 1.000 38.41 ATOM 7049 N PHE D 216 59.168 34.494 7.535 1.000 29.37 ATOM 7050 CA PHE D 216 60.509 34.039 7.173 1.000 32.74 ATOM 7051 CE PHE D 216 61.264 35.120 6.393 1.000 39.51 ATOM 7052 CG PHE D 216 62.718 34.703 6.173 1.000 50.14 ATOM 7053 CD1 PHE D 216 63.025 33.727 5.238 1.000 49.41 ATOM 7054 CD2 PHE D 216 63.742 35.278 6.902 1.000 50.29 ATOM 7055 CE1 PHE D 216 64.335 33.334 5.035 1.000 44.06 ATOM 7056 CE2 PHE D 216 65.054 34.893 6.701 1.000 46.56 ATOM 7057 CZ PHE D 216 65.348 33.918 5.769 1.000 46.69 ATOM 7058 C PHE D 216 61.305 33.649 8.414 1.000 39.85 ATOM 7059 O PHE D 216 62.079 32.688 8.442 1.000 30.19 ATOM 7060 N LEU D 217 61.137 34.418 9.490 1.000 37.21 ATOM 7061 CA LEU D 217 61.880 34.075 10.706 1.000 37.90 ATOM 7062 CE LEU D 217 61.666 35.177 11.744 1.000 34.46 ATOM 7063 CG LEU D 217 62.236 36.544 11.361 1.000 39.81 ATOM 7064 CD1 LEU D 217 61.332 37.662 11.855 1.000 60.47 ATOM 7065 CD2 LEU D 217 63.649 36.688 11.905 1.000 46.98 ATOM 7066 C LEU D 217 61.451 32.719 11.245 1.000 36.78 ATOM 7067 O LEU D 217 62.230 31.827 11.578 1.000 29.88 ATOM 7068 N ALA D 218 60.133 32.559 11.332 1.000 43.92 ATOM 7069 CA ALA D 218 59.557 31.298 11.776 1.000 43.98 ATOM 7070 CE ALA D 218 58.040 31.379 11.691 1.000 38.83 ATOM 7071 C ALA D 218 60.094 30.130 10.954 1.000 40.99 ATOM 7072 O ALA D 218 60.383 29.067 11.503 1.000 32.70 ATOM 7073 N SER D 219 60.227 30.335 9.647 1.000 34.44 ATOM 7074 CA SER D 219 60.633 29.263 8.743 1.000 35.59 ATOM 7075 CB SER D 219 60.428 29.707 7.285 1.000 23.01 ATOM 7076 OG SER D 219 61.418 30.652 6.916 1.000 30.06 ATOM 7077 CB SER D 219 62.072 28.823 8.963 1.000 33.93 ATOM 7078 O SER D 219 62.477 27.748 8.509 1.000 33.39 ATOM 7079 N GLN D 220 62.897 29.608 9.655 1.000 30.98 ATOM 7080 CA GLN D 220 64.276 29.166 9.859 1.000 27.90 ATOM 7081 CB GLN D 220 65.195 30.396 9.853 1.000 36.24 ATOM 7082 CG GLN D 220 65.232 31.099 8.503 1.000 46.18 ATOM 7083 CD GLN D 220 66.163 30.411 7.518 1.000 54.81 ATOM 7084 OE1 GLN D 220 65.767 29.453 6.849 1.000 66.52 ATOM 7085 NE2 GLN D 220 67.395 30.899 7.444 1.000 60.18 ATOM 7086 C GLN D 220 64.496 28.378 11.136 1.000 28.60 ATOM 7087 O GLN D 220 65.625 27.979 11.455 1.000 28.34 ATOM 7088 N VAL D 221 63.440 28.128 11.908 1.000 25.05 ATOM 7089 CA VAL D 221 63.609 27.295 13.105 1.000 19.69 ATOM 7090 CB VAL D 221 62.413 27.458 14.059 1.000 20.39 ATOM 7091 CD1 VAL D 221 62.610 26.648 15.335 1.000 17.64 ATOM 7092 CG2 VAL D 221 62.203 28.931 14.383 1.000 18.24 ATOM 7093 C VAL D 221 63.780 25.845 12.681 1.000 23.22 ATOM 7094 O VAL D 221 62.887 25.317 12.012 1.000 24.53 ATOM 7095 N PRO D 222 64.880 25.184 13.016 1.000 24.73 ATOM 7096 CD PRO D 222 66.023 25.665 13.817 1.000 24.93 ATOM 7097 CA PRO D 222 65.088 23.800 12.563 1.000 21.41 ATOM 7098 CB PRO D 222 66.427 23.404 13.205 1.000 16.76 ATOM 7099 CG PRO D 222 67.124 24.722 13.388 1.000 21.93 ATOM 7100 C PRO D 222 64.003 22.834 13.008 1.000 29.64 ATOM 7101 O PRO D 222 63.404 22.156 12.161 1.000 28.28 ATOM 7102 N PHE D 223 63.736 22.722 14.313 1.000 23.80 ATOM 7103 CA PHE D 223 62.666 21.830 14.735 1.000 22.47 ATOM 7104 CB PHE D 223 63.024 20.345 14.635 1.000 23.46 ATOM 7105 CG PHE D 223 61.800 19.501 14.996 1.000 26.96 ATOM 7106 CD1 PHE D 223 60.745 19.389 14.106 1.000 27.25 ATOM 7107 CD2 PHE D 223 61.727 18.848 16.214 1.000 24.04 ATOM 7108 CE1 PHE D 223 59.625 18.638 14.426 1.000 26.15 ATOM 7109 CE2 PHE D 223 60.612 18.098 16.536 1.000 24.75 ATOM 7110 CZ PHE D 223 59.556 17.995 15.647 1.000 24.07 ATOM 7111 C PHE D 223 62.245 22.127 16.172 1.000 27.70 ATOM 7112 O PHE D 223 63.118 22.190 17.041 1.000 26.86 ATOM 7113 N PRO D 224 60.960 22.305 16.446 1.000 29.69 ATOM 7114 CD PRO D 224 60.423 22.503 17.808 1.000 28.64 ATOM 7115 CA PRO D 224 59.899 22.326 15.434 1.000 28.89 ATOM 7116 CB PRO D 224 58.618 22.234 16.255 1.000 31.37 ATOM 7117 CG PRO D 224 58.975 22.838 17.575 1.000 30.74 ATOM 7118 C PRO D 224 59.930 23.631 14.638 1.000 27.50 ATOM 7119 O PRO D 224 60.332 24.659 15.179 1.000 23.79 ATOM 7120 N SER D 225 59.562 23.535 13.368 1.000 26.30 ATOM 7121 CA SER D 225 59.718 24.654 12.448 1.000 30.56 ATOM 7122 CE SER D 225 59.863 24.205 10.995 1.000 39.18 ATOM 7123 OG SER D 225 60.424 22.921 10.825 1.000 56.39 ATOM 7124 CB SER D 225 58.529 25.608 12.578 1.000 29.67 ATOM 7125 O SER D 225 57.621 25.653 11.753 1.000 27.17 ATOM 7126 N ARG D 226 58.561 26.389 13.650 1.000 26.12 ATOM 7127 CA ARG D 226 57.502 27.349 13.938 1.000 23.63 ATOM 7128 CB ARG D 226 56.244 26.629 14.420 1.000 20.50 ATOM 7129 CG ARG D 226 56.534 25.671 15.576 1.000 19.56 ATOM 7130 CD ARG D 226 55.319 25.523 16.471 1.000 25.12 ATOM 7131 NE ARG D 226 55.428 24.429 17.437 1.000 24.67 ATOM 7132 CZ ARG D 226 55.846 24.588 18.692 1.000 26.53 ATOM 7133 NH1 ARG D 226 55.915 23.545 19.508 1.000 21.62 ATOM 7134 NR2 ARG D 226 56.198 25.789 19.128 1.000 22.97 ATOM 7135 C ARG D 226 57.985 28.311 15.012 1.000 25.88 ATOM 7136 O ARG D 226 59.002 28.034 15.650 1.000 27.19 ATOM 7137 N LEU D 227 57.272 29.410 15.216 1.000 22.50 ATOM 7138 CA LEU D 227 57.614 30.242 16.371 1.000 25.88 ATOM 7139 CB LEU D 227 56.803 31.533 16.326 1.000 26.52 ATOM 7140 CG LEU D 227 57.095 32.428 15.114 1.000 24.01 ATOM 7141 CD1 LEU D 227 56.142 33.614 15.088 1.000 22.93 ATOM 7142 CD2 LEU D 227 58.547 32.883 15.124 1.000 18.44 ATOM 7143 C LEU D 227 57.366 29.458 17.652 1.000 24.33 ATOM 7144 O LEU D 227 56.537 28.548 17.677 1.000 20.20 ATOM 7145 N GLY D 228 58.081 29.787 18.721 1.000 21.98 ATOM 7146 CA GLY D 228 57.837 29.125 19.996 1.000 20.07 ATOM 7147 C GLY D 228 56.496 29.562 20.569 1.000 20.67 ATOM 7148 O GLY D 228 56.058 30.683 20.327 1.000 25.18 ATOM 7149 N ASP D 229 55.840 28.688 21.311 1.000 21.96 ATOM 7150 CA ASP D 229 54.566 28.978 21.971 1.000 22.40 ATOM 7151 CB ASP D 229 53.751 27.696 22.030 1.000 25.51 ATOM 7152 CG ASP D 229 52.428 27.776 22.752 1.000 38.71 ATOM 7153 OD1 ASP D 229 51.577 26.898 22.478 1.000 53.25 ATOM 7154 OD2 ASP D 229 52.189 28.671 23.585 1.000 37.19 ATOM 7155 C ASP D 229 54.842 29.536 23.365 1.000 21.25 ATOM 7156 O ASP D 229 55.580 28.891 24.119 1.000 22.74 ATOM 7157 N PRO D 230 54.299 30.688 23.715 1.000 23.51 ATOM 7158 CD PRO D 230 53.440 31.547 22.877 1.000 25.76 ATOM 7159 CA PRO D 230 54.527 31.282 25.042 1.000 24.49 ATOM 7160 CB PRO D 230 53.474 32.399 25.093 1.000 24.44 ATOM 7161 CG PRO D 230 53.403 32.840 23.656 1.000 23.90 ATOM 7162 C PRO D 230 54.331 30.298 26.184 1.000 24.91 ATOM 7163 O PRO D 230 55.048 30.381 27.185 1.000 23.08 ATOM 7164 N ALA D 231 53.405 29.354 26.066 1.000 25.76 ATOM 7165 CA ALA D 231 53.263 28.311 27.083 1.000 25.88 ATOM 7166 CB ALA D 231 52.139 27.341 26.750 1.000 16.85 ATOM 7167 C ALA D 231 54.545 27.504 27.256 1.000 26.87 ATOM 7168 O ALA D 231 54.831 27.004 28.343 1.000 24.96 ATOM 7169 N GLU D 232 55.310 27.376 26.170 1.000 22.61 ATOM 7170 CA GLU D 232 56.565 26.623 26.239 1.000 22.59 ATOM 7171 CB GLU D 232 57.072 26.343 24.825 1.000 23.36 ATOM 7172 CG GLU D 232 56.259 25.290 24.103 1.000 22.39 ATOM 7173 CD GLU D 232 56.491 25.243 22.609 1.000 23.33 ATOM 7174 OE1 GLU D 232 56.947 26.228 21.994 1.000 24.03 ATOM 7175 OE2 GLU D 232 56.200 24.169 22.042 1.000 27.05 ATOM 7176 C GLU D 232 57.586 27.376 27.080 1.000 21.77 ATOM 7177 O GLU D 232 58.351 26.775 27.831 1.000 21.99 ATOM 7178 N TYR D 233 57.391 28.707 26.993 1.000 19.90 ATOM 7179 CA TYR D 233 58.405 29.480 27.927 1.000 20.05 ATOM 7180 CB TYR D 233 58.302 30.975 27.612 1.000 19.81 ATOM 7181 CG TYR D 233 59.053 31.863 28.575 1.000 21.66 ATOM 7182 CD1 TYR D 233 60.405 32.127 28.406 1.000 17.10 ATOM 7183 CE1 TYR D 233 61.093 32.938 29.284 1.000 17.27 ATOM 7184 CD2 TYR D 233 58.410 32.448 29.662 1.000 20.72 ATOM 7185 CE2 TYR D 233 59.098 33.258 30.543 1.000 21.75 ATOM 7186 CZ TYR D 233 60.437 33.503 30.355 1.000 19.73 ATOM 7187 OH TYR D 233 61.105 34.314 31.242 1.000 21.89 ATOM 7188 C TYR D 233 57.961 29.200 29.361 1.000 28.08 ATOM 7189 O TYR D 233 58.773 28.926 30.248 1.000 29.73 ATOM 7190 N ALA D 234 56.656 29.275 29.598 1.000 25.56 ATOM 7191 CA ALA D 234 56.071 29.079 30.922 1.000 19.98 ATOM 7192 CB ALA D 234 54.555 29.223 30.853 1.000 20.85 ATOM 7193 C ALA D 234 56.444 27.720 31.507 1.000 19.41 ATOM 7194 O ALA D 234 56.819 27.634 32.677 1.000 25.32 ATOM 7195 N HIS D 235 56.347 26.661 30.704 1.000 18.96 ATOM 7196 CA HIS D 235 56.787 25.340 31.116 1.000 19.06 ATOM 7197 CB HIS D 235 56.705 24.328 29.966 1.000 21.94 ATOM 7198 CG HIS D 235 57.338 23.000 30.265 1.000 24.66 ATOM 7199 CD2 HIS D 235 58.590 22.520 30.052 1.000 22.51 ATOM 7200 ND1 HIS D 235 56.639 21.962 30.849 1.000 27.58 ATOM 7201 CE1 HIS D 235 57.430 20.914 30.994 1.000 22.15 ATOM 7202 NE2 HIS D 235 58.625 21.232 30.516 1.000 26.23 ATOM 7203 C HIS D 235 58.223 25.382 31.632 1.000 25.27 ATOM 7204 O HIS D 235 58.518 24.777 32.666 1.000 28.14 ATOM 7205 N LEU D 236 59.126 26.059 30.917 1.000 22.13 ATOM 7206 CA LEU D 236 60.521 26.045 31.352 1.000 21.53 ATOM 7207 CB LEU D 236 61.454 26.669 30.313 1.000 21.08 ATOM 7208 CG LEU D 236 62.939 26.690 30.708 1.000 18.33 ATOM 7209 CD1 LEU D 236 63.415 25.289 31.058 1.000 15.49 ATOM 7210 CD2 LEU D 236 63.801 27.274 29.595 1.000 20.04 ATOM 7211 C LEU D 236 60.683 26.782 32.680 1.000 22.66 ATOM 7212 O LEU D 236 61.451 26.354 33.544 1.000 22.41 ATOM 7213 N VAL D 237 59.961 27.884 32.848 1.000 22.04 ATOM 7214 CA VAL D 237 59.983 28.619 34.110 1.000 19.35 ATOM 7215 CB VAL D 237 59.040 29.831 34.088 1.000 23.88 ATOM 7216 CG1 VAL D 237 58.862 30.404 35.490 1.000 24.78 ATOM 7217 CG2 VAL D 237 59.556 30.915 33.146 1.000 20.31 ATOM 7218 C VAL D 237 59.597 27.686 35.250 1.000 24.98 ATOM 7219 O VAL D 237 60.241 27.617 36.293 1.000 25.46 ATOM 7220 N GLN D 238 58.515 26.934 35.045 1.000 26.56 ATOM 7221 CA GLN D 238 58.071 25.992 36.061 1.000 23.40 ATOM 7222 CB GLN D 238 56.793 25.272 35.615 1.000 27.07 ATOM 7223 CG GLN D 238 56.445 24.107 36.536 1.000 35.35 ATOM 7224 CD GLN D 238 55.029 23.607 36.317 1.000 46.19 ATOM 7225 OE1 GLN D 238 54.174 24.356 35.832 1.000 45.64 ATOM 7226 NE2 GLN D 238 54.789 22.342 36.664 1.000 44.19 ATOM 7227 C GLN D 238 59.133 24.943 36.376 1.000 22.17 ATOM 7228 O GLN D 238 59.384 24.636 37.542 1.000 27.26 ATOM 7229 N ALA D 239 59.739 24.383 35.333 1.000 17.35 ATOM 7230 CA ALA D 239 60.759 23.354 35.530 1.000 17.80 ATOM 7231 CB ALA D 239 61.226 22.829 34.177 1.000 22.63 ATOM 7232 C ALA D 239 61.934 23.882 36.339 1.000 22.18 ATOM 7233 O ALA D 239 62.531 23.165 37.148 1.000 24.37 ATOM 7234 N ILE D 240 62.280 25.149 36.123 1.000 20.99 ATOM 7235 CA ILE D 240 63.384 25.757 36.870 1.000 25.46 ATOM 7236 CB ILE D 240 63.847 27.078 36.229 1.000 23.16 ATOM 7237 CG2 ILE D 240 64.781 27.836 37.160 1.000 20.68 ATOM 7238 CG1 ILE D 240 64.496 26.888 34.852 1.000 19.72 ATOM 7239 CD1 ILE D 240 64.804 28.190 34.147 1.000 22.08 ATOM 7240 C ILE D 240 62.977 26.005 38.318 1.000 28.16 ATOM 7241 O ILE D 240 63.778 25.837 39.241 1.000 22.51 ATOM 7242 N ILE D 241 61.718 26.410 38.512 1.000 21.64 ATOM 7243 CA ILE D 241 61.278 26.665 39.891 1.000 28.25 ATOM 7244 CB ILE D 241 59.868 27.273 39.917 1.000 27.90 ATOM 7245 CG2 ILE D 241 59.182 27.110 41.264 1.000 26.14 ATOM 7246 CG1 ILE D 241 59.842 28.752 39.508 1.000 22.68 ATOM 7247 CD1 ILE D 241 58.490 29.205 38.990 1.000 22.21 ATOM 7248 C ILE D 241 61.345 25.369 40.689 1.000 29.32 ATOM 7249 O ILE D 241 61.787 25.334 41.840 1.000 26.76 ATOM 7250 N GLU D 242 60.919 24.291 40.042 1.000 21.42 ATOM 7251 CA GLU D 242 60.801 22.989 40.655 1.000 23.60 ATOM 7252 CB GLU D 242 59.922 22.114 39.746 1.000 24.58 ATOM 7253 CG GLU D 242 58.454 22.521 39.744 1.000 26.39 ATOM 7254 CD GLU D 242 57.567 21.445 39.142 1.000 30.24 ATOM 7255 OE1 GLU D 242 56.334 21.526 39.303 1.000 39.48 ATOM 7256 OE2 GLU D 242 58.113 20.516 38.508 1.000 38.42 ATOM 7257 C GLU D 242 62.128 22.289 40.908 1.000 28.27 ATOM 7258 O GLU D 242 62.259 21.554 41.891 1.000 25.03 ATOM 7259 N ASN D 243 63.121 22.467 40.042 1.000 20.97 ATOM 7260 CA ASN D 243 64.362 21.711 40.207 1.000 21.86 ATOM 7261 CB ASN D 243 64.983 21.403 38.843 1.000 22.88 ATOM 7262 CG ASN D 243 66.147 20.435 38.957 1.000 22.69 ATOM 7263 OD1 ASN D 243 67.066 20.629 39.753 1.000 23.72 ATOM 7264 ND2 ASN D 243 66.104 19.391 38.158 1.000 18.75 ATOM 7265 C ASN D 243 65.360 22.460 41.078 1.000 26.32 ATOM 7266 O ASN D 243 65.862 23.517 40.692 1.000 24.83 ATOM 7267 N PRO D 244 65.642 21.918 42.259 1.000 25.17 ATOM 7268 CD PRO D 244 65.169 20.615 42.752 1.000 24.25 ATOM 7269 CA PRO D 244 66.474 22.616 43.236 1.000 21.82 ATOM 7270 CB PRO D 244 66.451 21.675 44.453 1.000 24.37 ATOM 7271 CG PRO D 244 65.267 20.792 44.243 1.000 27.61 ATOM 7272 C PRO D 244 67.922 22.825 42.819 1.000 20.75 ATOM 7273 O PRO D 244 68.605 23.663 43.408 1.000 19.99 ATOM 7274 N PHE D 245 68.429 22.091 41.830 1.000 23.06 ATOM 7275 CA PHE D 245 69.865 22.153 41.541 1.000 19.95 ATOM 7276 CB PHE D 245 70.400 20.720 41.389 1.000 21.93 ATOM 7277 CG PHE D 245 71.836 20.520 41.853 1.000 20.86 ATOM 7278 CD1 PHE D 245 72.829 20.123 40.974 1.000 16.58 ATOM 7279 CD2 PHE D 245 72.179 20.743 43.176 1.000 17.52 ATOM 7280 CE1 PHE D 245 74.133 19.956 41.402 1.000 20.48 ATOM 7281 CE2 PHE D 245 73.476 20.574 43.610 1.000 17.54 ATOM 7282 CZ PHE D 245 74.469 20.180 42.723 1.000 17.22 ATOM 7283 C PHE D 245 70.193 22.997 40.319 1.000 25.51 ATOM 7284 O PHE D 245 71.362 23.052 39.917 1.000 21.54 ATOM 7285 N LEU D 246 69.233 23.672 39.703 1.000 23.04 ATOM 7286 CA LEU D 246 69.482 24.581 38.593 1.000 21.38 ATOM 7287 CB LEU D 246 68.263 24.699 37.661 1.000 20.45 ATOM 7288 CG LEU D 246 68.043 23.564 36.661 1.000 24.84 ATOM 7289 CD1 LEU D 246 66.692 23.681 35.969 1.000 21.22 ATOM 7290 CD2 LEU D 246 69.174 23.543 35.631 1.000 21.12 ATOM 7291 C LEU D 246 69.832 25.969 39.114 1.000 21.29 ATOM 7292 O LEU D 246 68.995 26.664 39.697 1.000 21.82 ATOM 7293 N ASN D 247 71.059 26.414 38.900 1.000 17.26 ATOM 7294 CA ASN D 247 71.489 27.713 39.389 1.000 18.30 ATOM 7295 CB ASN D 247 71.856 27.597 40.880 1.000 23.01 ATOM 7296 CG ASN D 247 71.921 28.933 41.591 1.000 27.53 ATOM 7297 OD1 ASN D 247 71.495 29.959 41.059 1.000 21.47 ATOM 7298 ND2 ASN D 247 72.465 28.964 42.807 1.000 21.65 ATOM 7299 C ASN D 247 72.678 28.254 38.597 1.000 18.72 ATOM 7300 O ASN D 247 73.562 27.492 38.201 1.000 19.15 ATOM 7301 N GLY D 248 72.714 29.563 38.391 1.000 18.94 ATOM 7302 CA GLY D 248 73.794 30.276 37.752 1.000 19.96 ATOM 7303 C GLY D 248 73.964 29.984 36.278 1.000 22.95 ATOM 7304 O GLY D 248 75.043 30.179 35.703 1.000 20.62 ATOM 7305 N GLU D 249 72.902 29.517 35.635 1.000 17.77 ATOM 7306 CA GLU D 249 73.018 29.050 34.253 1.000 15.96 ATOM 7307 CB GLU D 249 72.851 27.529 34.256 1.000 17.48 ATOM 7308 CG GLU D 249 72.390 26.859 32.984 1.000 16.91 ATOM 7309 CD GLU D 249 73.427 26.784 31.889 1.000 19.08 ATOM 7310 OE1 GLU D 249 73.463 25.784 31.143 1.000 22.69 ATOM 7311 OE2 GLU D 249 74.224 27.732 31.777 1.000 21.40 ATOM 7312 C GLU D 249 72.020 29.759 33.348 1.000 22.60 ATOM 7313 O GLU D 249 71.012 30.307 33.796 1.000 17.66 ATOM 7314 N VAL D 250 72.327 29.756 32.053 1.000 19.97 ATOM 7315 CA VAL D 250 71.486 30.277 30.994 1.000 15.24 ATOM 7316 CB VAL D 250 72.245 31.284 30.115 1.000 22.54 ATOM 7317 CG1 VAL D 250 71.343 31.787 28.994 1.000 19.92 ATOM 7318 CG2 VAL D 250 72.767 32.445 30.941 1.000 19.32 ATOM 7319 C VAL D 250 70.976 29.127 30.124 1.000 19.92 ATOM 7320 O VAL D 250 71.768 28.270 29.725 1.000 19.42 ATOM 7321 N ILE D 251 69.679 29.091 29.826 1.000 16.97 ATOM 7322 CA ILE D 251 69.132 27.997 29.033 1.000 20.11 ATOM 7323 CB ILE D 251 68.074 27.197 29.821 1.000 19.46 ATOM 7324 CG2 ILE D 251 67.514 26.093 28.930 1.000 19.68 ATOM 7325 CG1 ILE D 251 68.593 26.668 31.158 1.000 13.76 ATOM 7326 CD1 ILE D 251 67.692 25.683 31.850 1.000 17.14 ATOM 7327 C ILE D 251 68.500 28.495 27.738 1.000 18.55 ATOM 7328 O ILE D 251 67.578 29.312 27.763 1.000 20.22 ATOM 7329 N ARG D 252 69.005 27.995 26.614 1.000 21.00 ATOM 7330 CA ARG D 252 68.451 28.372 25.316 1.000 20.07 ATOM 7331 CB ARG D 252 69.442 28.127 24.185 1.000 20.58 ATOM 7332 CG ARG D 252 70.728 28.928 24.222 1.000 22.33 ATOM 7333 CD ARG D 252 71.650 28.523 23.073 1.000 21.13 ATOM 7334 NE ARG D 252 71.050 28.861 21.784 1.000 18.85 ATOM 7335 CZ ARG D 252 71.557 29.701 20.900 1.000 18.85 ATOM 7336 NH1 ARG D 252 70.918 29.927 19.764 1.000 16.90 ATOM 7337 NH2 ARG D 252 72.699 30.323 21.132 1.000 20.07 ATOM 7338 C ARG D 252 67.172 27.578 25.040 1.000 19.42 ATOM 7339 O ARG D 252 67.152 26.351 25.152 1.000 17.60 ATOM 7340 N LEU D 253 66.114 28.290 24.675 1.000 17.77 ATOM 7341 CA LEU D 253 64.837 27.685 24.320 1.000 17.55 ATOM 7342 CB LEU D 253 63.789 28.077 25.359 1.000 20.36 ATOM 7343 CG LEU D 253 62.383 27.489 25.190 1.000 19.52 ATOM 7344 CD1 LEU D 253 62.424 25.980 25.318 1.000 12.98 ATOM 7345 CD2 LEU D 253 61.427 28.098 26.216 1.000 17.81 ATOM 7346 C LEU D 253 64.464 28.176 22.925 1.000 22.27 ATOM 7347 O LEU D 253 63.866 29.242 22.798 1.000 18.37 ATOM 7348 N ASP D 254 64.845 27.447 21.875 1.000 17.63 ATOM 7349 CA ASP D 254 64.848 28.079 20.561 1.000 19.74 ATOM 7350 CB ASP D 254 66.170 28.856 20.403 1.000 16.22 ATOM 7351 CG ASP D 254 67.383 27.959 20.577 1.000 21.64 ATOM 7352 OD1 ASP D 254 67.232 26.720 20.613 1.000 18.65 ATOM 7353 OD2 ASP D 254 68.520 28.473 20.878 1.000 23.91 ATOM 7354 C ASP D 254 64.726 27.139 19.378 1.000 20.09 ATOM 7355 O ASP D 254 65.018 27.559 18.255 1.000 22.74 ATOM 7356 N GLY D 255 64.305 25.897 19.582 1.000 22.35 ATOM 7357 CA GLY D 255 64.101 24.976 18.468 1.000 18.23 ATOM 7358 C GLY D 255 65.387 24.678 17.715 1.000 23.86 ATOM 7359 O GLY D 255 65.338 24.219 16.567 1.000 21.75 ATOM 7360 N ALA D 256 66.502 24.941 18.375 1.000 19.53 ATOM 7361 CA ALA D 256 67.855 24.721 17.891 1.000 20.22 ATOM 7362 CB ALA D 256 67.986 23.287 17.391 1.000 19.78 ATOM 7363 C ALA D 256 68.267 25.702 16.802 1.000 22.63 ATOM 7364 O ALA D 256 69.219 25.455 16.056 1.000 21.69 ATOM 7365 N ILE D 257 67.569 26.833 16.682 1.000 19.23 ATOM 7366 CA ILE D 257 67.982 27.829 15.698 1.000 16.07 ATOM 7367 CB ILE D 257 66.915 28.924 15.518 1.000 18.79 ATOM 7368 CG2 ILE D 257 66.903 29.894 16.692 1.000 22.52 ATOM 7369 CG1 ILE D 257 67.039 29.710 14.207 1.000 16.43 ATOM 7370 CD1 ILE D 257 65.990 30.785 14.047 1.000 16.38 ATOM 7371 C ILE D 257 69.300 28.484 16.102 1.000 25.38 ATOM 7372 O ILE D 257 69.626 28.535 17.284 1.000 21.27 ATOM 7373 N ARG D 258 70.040 28.974 15.122 1.000 21.25 ATOM 7374 CA ARG D 258 71.191 29.848 15.281 1.000 17.34 ATOM 7375 CE ARG D 258 72.497 29.119 14.962 1.000 18.94 ATOM 7376 CG ARG D 258 72.797 27.932 15.880 1.000 17.46 ATOM 7377 CD ARD D 258 72.975 28.415 17.307 1.000 22.03 ATOM 7378 NE ARD D 258 73.280 27.368 18.263 1.000 22.14 ATOM 7379 CZ ARD D 258 72.412 26.609 18.913 1.000 24.72 ATOM 7380 NE1 ARG D 258 72.883 25.698 19.764 1.000 20.30 ATOM 7381 NH2 ARG D 258 71.104 26.745 18.728 1.000 19.58 ATOM 7382 C ARG D 258 70.997 31.053 14.369 1.000 23.77 ATOM 7383 O ARD D 258 70.781 30.903 13.156 1.000 24.03 ATOM 7384 N MET D 259 71.039 32.278 14.888 1.000 21.77 ATOM 7385 CA MET D 259 70.662 33.390 14.014 1.000 25.38 ATOM 7386 CB MET D 259 70.191 34.592 14.839 1.000 24.28 ATOM 7387 CD MET D 259 69.122 34.266 15.865 1.000 23.82 ATOM 7388 SD MET D 259 67.734 33.346 15.167 1.000 28.80 ATOM 7389 CE MET D 259 66.976 34.600 14.133 1.000 26.61 ATOM 7390 C MET D 259 71.794 33.830 13.091 1.000 30.90 ATOM 7391 O MET D 259 72.937 34.018 13.496 1.000 30.51 ATOM 7392 N GLN D 260 71.450 34.025 11.828 1.000 30.38 ATOM 7393 CA GLN D 260 72.343 34.553 10.806 1.000 25.30 ATOM 7394 CE GLN D 260 71.913 33.950 9.466 1.000 30.57 ATOM 7395 CD GLN D 260 72.719 32.746 9.023 1.000 43.46 ATOM 7396 CD GLN D 260 74.004 32.515 9.785 1.000 50.86 ATOM 7397 OE1 GLN D 260 75.109 32.788 9.311 1.000 41.52 ATOM 7398 NE2 GLN D 260 73.899 32.001 11.006 1.000 68.66 ATOM 7399 C GLN D 260 72.308 36.073 10.795 1.000 24.41 ATOM 7400 O GLN D 260 71.451 36.657 11.475 1.000 20.57 ATOM 7401 N PRO D 261 73.191 36.756 10.080 1.000 24.38 ATOM 7402 CD PRO D 261 74.281 36.227 9.234 1.000 26.73 ATOM 7403 CA PRO D 261 73.183 38.228 10.080 1.000 22.57 ATOM 7404 CB PRO D 261 74.205 38.582 8.992 1.000 23.87 ATOM 7405 CD PRO D 261 75.174 37.436 9.068 1.000 25.59 ATOM 7406 C PRO D 261 71.814 38.793 9.723 1.000 25.02 ATOM 7407 OT1 PRO D 261 71.101 38.072 9.000 1.000 27.55 ATOM 7408 OT2 PRO D 261 71.488 39.902 10.183 1.000 22.37 ATOM 7409 PN LIG D 262 57.422 39.435 25.068 1.000 23.15 ATOM 7410 O1N LIG D 262 57.806 38.514 23.885 1.000 25.67 ATOM 7411 O2N LIG D 262 56.360 38.756 25.925 1.000 26.40 ATOM 7412 O3P LIG D 262 56.913 40.769 24.463 1.000 23.02 ATOM 7413 OSM LIG D 262 58.744 39.749 25.910 1.000 24.23 ATOM 7414 C5M LIG D 262 59.075 39.020 27.127 1.000 18.88 ATOM 7415 C4M LIG D 262 60.636 38.980 27.309 1.000 18.29 ATOM 7416 O4M LIG D 262 61.167 38.014 26.391 1.000 22.02 ATOM 7417 C3M LIG D 262 61.315 40.324 26.955 1.000 18.81 ATOM 7418 O3M LIG D 262 62.389 40.543 27.900 1.000 22.74 ATOM 7419 C2M LIG D 262 61.878 40.076 25.532 1.000 14.35 ATOM 7420 O2M LIG D 262 62.962 41.002 25.316 1.000 20.42 ATOM 7421 C1M LIG D 262 62.259 38.591 25.613 1.000 20.56 ATOM 7422 N1N LIG D 262 62.462 37.840 24.339 1.000 22.42 ATOM 7423 C6N LIG D 262 63.798 37.319 24.034 1.000 25.78 ATOM 7424 C5N LIG D 262 64.040 36.661 22.882 1.000 26.30 ATOM 7425 C4N LIG D 262 62.985 36.644 21.748 1.000 26.65 ATOM 7426 C3N LIG D 262 61.541 36.889 22.299 1.000 22.98 ATOM 7427 C2N LIG D 262 61.342 37.606 23.421 1.000 23.56 ATOM 7428 C7N LIG D 262 60.403 36.620 21.333 1.000 20.05 ATOM 7429 O7N LIG D 262 60.607 36.003 20.279 1.000 22.45 ATOM 7430 N7N LIG D 262 59.213 37.076 21.680 1.000 14.14 ATOM 7431 PA LIG D 262 55.631 41.515 24.912 1.000 26.46 ATOM 7432 O1A LIG D 262 55.631 42.919 24.316 1.000 24.54 ATOM 7433 O2A LIG D 262 54.364 40.750 24.508 1.000 29.61 ATOM 7434 O5B LIG D 262 55.637 41.666 26.507 1.000 26.93 ATOM 7435 C5B LIG D 262 56.576 42.588 27.145 1.000 20.55 ATOM 7436 C4B LIG D 262 55.898 43.240 28.393 1.000 23.80 ATOM 7437 O4B LIG D 262 56.880 44.008 29.138 1.000 21.67 ATOM 7438 C3B LIG D 262 54.724 44.179 27.988 1.000 24.11 ATOM 7439 O3B LIG D 262 53.525 43.815 28.694 1.000 22.60 ATOM 7440 C2B LIG D 262 55.237 45.558 28.426 1.000 28.11 ATOM 7441 O2B LIG D 262 54.192 46.481 28.755 1.000 27.28 ATOM 7442 C1B LIG D 262 56.225 45.221 29.568 1.000 19.96 ATOM 7443 N9A LIG D 262 57.210 46.336 29.738 1.000 22.28 ATOM 7444 C4A LIG D 262 57.558 46.962 30.940 1.000 20.80 ATOM 7445 N3A LIG D 262 57.133 46.764 32.324 1.000 19.84 ATOM 7446 C2A LIG D 262 57.705 47.570 33.190 1.000 15.71 ATOM 7447 N1A LIG D 262 58.594 48.507 32.971 1.000 24.24 ATOM 7448 C6A LIG D 262 59.043 48.762 31.754 1.000 20.94 ATOM 7449 C5A LIG D 262 58.541 47.990 30.639 1.000 23.41 ATOM 7450 N7A LIG D 262 58.836 48.041 29.278 1.000 30.14 ATOM 7451 C8A LIG D 262 58.005 47.040 28.846 1.000 21.02 ATOM 7452 N6A LIG D 262 59.761 49.860 31.547 1.000 18.74 ATOM 7453 C LIG D 262 63.468 42.004 16.293 1.000 37.19 ATOM 7454 C1 LIG D 262 64.908 42.400 15.731 1.000 40.91 ATOM 7455 N LIG D 262 65.122 42.614 14.374 1.000 46.58 ATOM 7456 O LIG D 262 65.816 42.505 16.583 1.000 32.75 ATOM 7457 C2 LIG D 262 63.981 42.485 13.406 1.000 51.55 ATOM 7458 C3 LIG D 262 63.916 41.176 12.560 1.000 55.49 ATOM 7459 C4 LIG D 262 66.506 42.952 13.906 1.000 38.70 ATOM 7460 C5 LIG D 262 67.250 41.676 13.422 1.000 39.77 ATOM 7461 C6 LIG D 262 66.495 40.887 12.339 1.000 43.74 ATOM 7462 C7 LIG D 262 65.145 40.259 12.747 1.000 52.09 ATOM 7463 C8 LIG D 262 62.498 43.226 16.479 1.000 26.51 ATOM 7464 C9 LIG D 262 61.135 42.962 16.665 1.000 35.63 ATOM 7465 C10 LIG D 262 60.228 44.006 16.841 1.000 32.64 ATOM 7466 C11 LIG D 262 60.671 45.323 16.828 1.000 28.46 ATOM 7467 C12 LIG D 262 62.026 45.594 16.657 1.000 31.49 ATOM 7468 C13 LIG D 262 62.930 44.554 16.461 1.000 24.95 ATOM 7469 C15 LIG D 262 63.762 41.769 18.722 1.000 32.41 ATOM 7470 N1 LIG D 262 63.815 41.274 19.918 1.000 31.72 ATOM 7471 C16 LIG D 262 63.550 39.860 20.066 1.000 31.24 ATOM 7472 C17 LIG D 262 63.243 39.052 18.946 1.000 27.85 ATOM 7473 C18 LIG D 262 63.219 39.705 17.545 1.000 34.74 ATOM 7474 N2 LIG D 262 63.493 41.175 17.586 1.000 39.88 ATOM 7475 S LIG D 262 62.871 38.731 16.107 1.000 32.53 ATOM 7476 C19 LIG D 262 63.019 37.761 19.346 1.000 27.53 ATOM 7477 N3 LIG D 262 63.217 37.741 20.731 1.000 33.77 ATOM 7478 N4 LIG D 262 63.516 39.014 21.153 1.000 30.88 ATOM 7479 O HOH 301 92.776 12.297 31.743 1.000 20.14 ATOM 7480 O HOH 302 77.559 34.144 9.282 1.000 20.43 ATOM 7481 O HOH 303 80.425 29.345 40.907 1.000 16.20 ATOM 7482 O HOH 304 91.952 31.264 29.002 1.000 16.74 ATOM 7483 O HOH 305 94.801 36.551 34.544 1.000 22.14 ATOM 7484 O HOH 306 65.211 42.139 29.804 1.000 22.38 ATOM 7485 O HOH 307 100.866 4.606 25.942 1.000 22.10 ATOM 7486 O HOH 308 70.380 25.625 13.725 1.000 25.15 ATOM 7487 O HOH 309 98.836 38.721 8.048 1.000 20.62 ATOM 7488 O HOH 310 73.571 6.226 35.060 1.000 32.14 ATOM 7489 O HOH 311 88.880 24.223 27.409 1.000 20.29 ATOM 7490 O HOH 312 72.760 24.489 37.007 1.000 18.84 ATOM 7491 O HOH 313 94.756 19.229 14.119 1.000 26.27 ATOM 7492 O HOH 314 87.327 22.157 29.706 1.000 16.82 ATOM 7493 O HOH 315 63.431 29.981 17.877 1.000 23.03 ATOM 7494 O HOH 316 84.014 35.114 15.138 1.000 20.55 ATOM 7495 O HOH 317 87.485 35.486 13.797 1.000 25.53 ATOM 7496 O HOH 318 83.964 52.541 27.664 1.000 18.55 ATOM 7497 O HOH 319 77.741 41.945 42.922 1.000 16.89 ATOM 7498 O HOH 320 93.152 52.197 29.838 1.000 24.83 ATOM 7499 O HOH 321 97.176 7.390 32.191 1.000 25.52 ATOM 7500 O HOH 322 77.957 35.854 11.120 1.000 18.59 ATOM 7501 O HOH 323 85.629 53.769 25.435 1.000 18.98 ATOM 7502 O HOH 324 86.538 32.202 24.492 1.000 40.93 ATOM 7503 O HOH 325 87.007 49.918 27.784 1.000 27.18 ATOM 7504 O HOH 326 77.600 20.706 41.125 1.000 21.42 ATOM 7505 O HOH 327 78.902 55.159 40.598 1.000 42.52 ATOM 7506 O HOH 328 81.133 17.266 35.954 1.000 23.52 ATOM 7507 O HOH 329 113.031 19.892 24.590 1.000 29.70 ATOM 7508 O HOH 330 104.459 32.288 29.421 1.000 22.61 ATOM 7509 O HOH 331 78.966 10.036 27.642 1.000 28.79 ATOM 7510 O HOH 332 82.521 27.789 41.932 1.000 24.45 ATOM 7511 O HOH 333 78.816 22.190 17.044 1.000 21.49 ATOM 7512 O HOH 334 90.214 12.158 32.342 1.000 19.15 ATOM 7513 O HOH 335 75.406 27.047 28.515 1.000 46.66 ATOM 7514 O HOH 336 67.009 36.757 18.236 1.000 29.57 ATOM 7515 O HOH 337 88.708 40.365 34.712 1.000 20.85 ATOM 7516 O HOH 338 61.508 16.582 41.397 1.000 29.21 ATOM 7517 O HOH 339 79.952 36.047 34.651 1.000 22.65 ATOM 7518 O HOH 340 69.698 25.567 20.952 1.000 20.27 ATOM 7519 O HOH 341 78.040 6.743 26.436 1.000 16.46 ATOM 7520 O HOH 342 112.979 15.545 31.632 1.000 32.19 ATOM 7521 O HOH 343 76.376 14.721 10.758 1.000 27.36 ATOM 7522 O HOH 344 69.396 52.971 44.875 1.000 19.26 ATOM 7523 O HOH 345 94.466 33.698 27.831 1.000 18.87 ATOM 7524 O HOH 346 62.211 43.111 34.699 1.000 18.14 ATOM 7525 O HOH 347 79.228 32.834 46.344 1.000 25.33 ATOM 7526 O HOH 348 91.707 29.243 37.874 1.000 22.18 ATOM 7527 O HOH 349 95.704 15.420 15.073 1.000 24.76 ATOM 7528 O HOH 350 63.929 53.848 21.940 1.000 39.40 ATOM 7529 O HOH 351 80.675 45.514 39.966 1.000 17.96 ATOM 7530 O HOH 352 78.369 45.158 41.405 1.000 23.26 ATOM 7531 O HOH 353 55.124 29.871 13.566 1.000 26.74 ATOM 7532 O HOH 354 85.117 31.485 28.658 1.000 32.69 ATOM 7533 O HOH 355 75.734 38.342 20.028 1.000 24.32 ATOM 7534 O HOH 356 74.602 22.606 21.931 1.000 23.88 ATOM 7535 O HOH 357 81.874 37.548 19.721 1.000 17.64 ATOM 7536 O HOH 358 63.070 49.539 15.889 1.000 30.23 ATOM 7537 O HOH 359 98.248 16.502 15.469 1.000 17.16 ATOM 7538 O HOH 360 76.327 11.060 26.671 1.000 24.63 ATOM 7539 O HOH 361 74.997 29.485 22.470 1.000 39.59 ATOM 7540 O HOH 362 104.920 40.576 24.671 1.000 31.70 ATOM 7541 O HOH 363 79.230 38.710 20.312 1.000 29.49 ATOM 7542 O HOH 364 99.247 52.723 33.905 1.000 35.67 ATOM 7543 O HOH 365 63.759 24.391 44.403 1.000 34.65 ATOM 7544 O HOH 366 48.099 14.793 14.578 1.000 36.68 ATOM 7545 O HOH 367 55.097 3.198 34.387 1.000 37.64 ATOM 7546 O HOH 368 66.645 44.792 48.647 1.000 31.11 ATOM 7547 O HOH 369 78.813 0.682 11.091 1.000 25.32 ATOM 7548 O HOH 370 116.182 20.584 26.457 1.000 42.78 ATOM 7549 O HOH 371 72.392 60.443 19.265 1.000 27.98 ATOM 7550 O HOH 372 85.512 19.921 35.425 1.000 26.77 ATOM 7551 O HOH 373 75.463 31.905 33.759 1.000 30.07 ATOM 7552 O HOH 374 79.323 7.223 7.370 1.000 25.70 ATOM 7553 O HOH 375 82.491 27.441 44.754 1.000 27.05 ATOM 7554 O HOH 376 86.109 27.617 30.944 1.000 27.46 ATOM 7555 O HOH 377 43.566 47.081 32.187 1.000 16.13 ATOM 7556 O HOH 378 103.241 48.462 25.650 1.000 24.71 ATOM 7557 O HOH 379 69.968 37.248 17.438 1.000 23.41 ATOM 7558 O HOH 380 89.350 26.980 26.742 1.000 20.25 ATOM 7559 O HOH 381 51.634 43.602 24.654 1.000 30.52 ATOM 7560 O HOH 382 114.006 8.766 15.300 1.000 24.65 ATOM 7561 O HOH 383 84.217 48.991 29.017 1.000 31.07 ATOM 7562 O HOH 384 91.931 27.844 35.321 1.000 17.17 ATOM 7563 O HOH 385 85.192 48.196 25.874 1.000 29.60 ATOM 7564 O HOH 386 115.322 21.322 4.709 1.000 20.42 ATOM 7565 O HOH 387 66.453 24.956 22.897 1.000 29.29 ATOM 7566 O HOH 388 56.086 39.303 28.854 1.000 22.55 ATOM 7567 O HOH 389 79.289 8.651 45.437 1.000 42.77 ATOM 7568 O HOH 390 76.016 49.742 45.810 1.000 27.62 ATOM 7569 O HOH 391 69.096 54.578 16.314 1.000 19.36 ATOM 7570 O HOH 392 79.524 40.851 4.029 1.000 35.85 ATOM 7571 O HOH 393 97.800 21.307 7.889 1.000 18.96 ATOM 7572 O HOH 394 60.387 3.283 17.265 1.000 39.16 ATOM 7573 O HOH 395 70.626 54.803 43.647 1.000 26.49 ATOM 7574 O HOH 396 82.133 24.094 23.840 1.000 32.45 ATOM 7575 O HOH 397 79.984 13.271 10.506 1.000 31.95 ATOM 7576 O HOH 398 69.755 27.539 12.357 1.000 19.92 ATOM 7577 O HOH 399 54.427 53.254 36.600 1.000 31.14 ATOM 7578 O HOH 400 76.245 41.299 7.666 1.000 32.49 ATOM 7579 O HOH 401 102.361 4.194 11.337 1.000 32.26 ATOM 7580 O HOH 402 65.368 39.607 32.062 1.000 18.45 ATOM 7581 O HOH 403 77.627 33.285 17.947 1.000 32.18 ATOM 7582 O HOH 404 84.225 68.543 24.460 1.000 30.38 ATOM 7583 O HOH 405 106.651 33.242 30.436 1.000 26.95 ATOM 7584 O HOH 406 75.077 45.385 49.011 1.000 29.52 ATOM 7585 O HOH 407 79.455 27.085 30.595 1.000 46.96 ATOM 7586 O HOH 408 51.139 29.211 29.538 1.000 21.79 ATOM 7587 O HOH 409 64.552 55.161 40.457 1.000 29.93 ATOM 7588 O HOH 410 107.550 27.293 35.489 1.000 30.38 ATOM 7589 O HOH 411 53.653 44.875 20.990 1.000 42.39 ATOM 7590 O HOH 412 68.940 50.613 10.578 1.000 33.53 ATOM 7591 O HOH 413 77.823 37.269 27.398 1.000 52.66 ATOM 7592 O HOH 414 88.020 33.385 −1.498 1.000 23.87 ATOM 7593 O HOH 415 73.543 9.125 6.557 1.000 37.72 ATOM 7594 O HOH 416 58.879 47.725 48.958 1.000 29.83 ATOM 7595 O HOH 417 76.336 65.330 23.962 1.000 22.36 ATOM 7596 O HOH 418 52.443 49.100 42.295 1.000 24.67 ATOM 7597 O HOH 419 70.535 6.347 41.406 1.000 27.74 ATOM 7598 O HOH 420 88.288 67.546 11.973 1.000 30.11 ATOM 7599 O HOH 421 69.212 56.275 41.596 1.000 32.93 ATOM 7600 O HOH 422 64.777 −7.683 32.662 1.000 39.39 ATOM 7601 O HOH 423 85.507 37.769 37.127 1.000 26.18 ATOM 7602 O HOH 424 60.769 −5.497 35.178 1.000 35.95 ATOM 7603 O HOH 425 76.724 9.020 28.963 1.000 26.73 ATOM 7604 O HOH 426 88.772 58.307 9.168 1.000 35.00 ATOM 7605 O HOH 427 92.867 17.963 14.820 1.000 24.96 ATOM 7606 O HOH 428 46.765 52.287 25.746 1.000 31.05 ATOM 7607 O HOH 429 84.460 45.572 38.946 1.000 32.72 ATOM 7608 O HOH 430 75.187 5.894 25.803 1.000 23.00 ATOM 7609 O HOH 431 59.372 37.396 51.274 1.000 25.28 ATOM 7610 O HOH 432 90.348 42.583 7.062 1.000 24.06 ATOM 7611 O HOH 433 59.054 18.728 19.491 1.000 26.20 ATOM 7612 O HOH 434 87.471 8.190 6.913 1.000 38.33 ATOM 7613 O HOH 435 57.945 16.732 23.289 1.000 40.80 ATOM 7614 O HOH 436 63.529 44.279 32.431 1.000 19.37 ATOM 7615 O HOH 437 101.843 39.707 39.930 1.000 28.87 ATOM 7616 O HOH 438 64.407 24.039 48.731 1.000 37.91 ATOM 7617 O HOH 439 88.442 7.691 52.002 1.000 42.77 ATOM 7618 O HOH 440 72.465 31.064 44.572 1.000 21.67 ATOM 7619 O HOH 441 68.994 41.346 10.123 1.000 42.94 ATOM 7620 O HOH 442 79.097 44.850 49.113 1.000 29.22 ATOM 7621 O HOH 443 54.574 41.823 5.022 1.000 43.31 ATOM 7622 O HOH 444 62.894 40.739 30.750 1.000 27.05 ATOM 7623 O HOH 445 87.850 39.681 37.054 1.000 29.04 ATOM 7624 O HOH 446 102.935 6.383 30.051 1.000 26.13 ATOM 7625 O HOH 447 81.399 0.725 10.978 1.000 31.16 ATOM 7626 O HOH 448 75.791 2.055 7.947 1.000 36.53 ATOM 7627 O HOH 449 70.507 48.423 17.926 1.000 20.58 ATOM 7628 O HOH 450 105.650 12.383 27.890 1.000 26.46 ATOM 7629 O HOH 451 82.895 43.409 9.910 1.000 20.55 ATOM 7630 O HOH 452 110.272 15.926 31.003 1.000 26.86 ATOM 7631 O HOH 453 68.815 46.589 18.947 1.000 21.05 ATOM 7632 O HOH 454 76.594 34.173 33.922 1.000 26.38 ATOM 7633 O HOH 455 54.072 46.868 24.653 1.000 30.30 ATOM 7634 O HOH 456 91.069 42.715 4.402 1.000 27.91 ATOM 7635 O HOH 457 81.997 14.819 10.048 1.000 20.02 ATOM 7636 O HOH 458 67.486 23.662 48.188 1.000 22.81 ATOM 7637 O HOH 459 52.296 49.095 47.652 1.000 25.11 ATOM 7638 O HOH 460 75.602 26.828 36.321 1.000 24.34 ATOM 7639 O HOH 461 77.276 34.990 6.677 1.000 21.15 ATOM 7640 O HOH 462 58.803 46.498 21.948 1.000 46.48 ATOM 7641 O HOH 463 65.913 54.952 36.668 1.000 45.96 ATOM 7642 O HOH 464 86.907 10.226 56.341 1.000 49.82 ATOM 7643 O HOH 465 75.050 24.660 23.343 1.000 30.62 ATOM 7644 O HOH 466 85.073 24.898 42.520 1.000 33.55 ATOM 7645 O HOH 467 100.013 26.261 2.735 1.000 25.57 ATOM 7646 O HOH 468 102.785 31.581 6.162 1.000 30.61 ATOM 7647 O HOH 469 89.302 53.313 35.809 1.000 30.13 ATOM 7648 O HOH 470 99.425 16.286 2.376 1.000 26.49 ATOM 7649 O HOH 471 54.696 54.570 33.861 1.000 24.27 ATOM 7650 O HOH 472 66.678 17.442 45.628 1.000 36.63 ATOM 7651 O HOH 473 88.323 39.792 39.649 1.000 29.12 ATOM 7652 O HOH 474 75.968 30.164 31.264 1.000 23.90 ATOM 7653 O HOH 475 76.155 27.321 18.568 1.000 38.98 ATOM 7654 O HOH 476 101.777 17.659 38.545 1.000 38.91 ATOM 7655 O HOH 477 54.564 21.181 19.102 1.000 36.10 ATOM 7656 O HOH 478 85.523 31.838 7.876 1.000 22.22 ATOM 7657 O HOH 479 100.112 10.630 34.314 1.000 37.69 ATOM 7658 O HOH 480 82.501 35.202 20.962 1.000 25.05 ATOM 7659 O HOH 481 102.572 64.683 21.745 1.000 26.48 ATOM 7660 O HOH 482 73.557 38.100 49.865 1.000 32.24 ATOM 7661 O HOH 483 114.148 7.806 13.007 1.000 26.89 ATOM 7662 O HOH 484 44.492 43.400 40.299 1.000 32.81 ATOM 7663 O HOH 485 74.717 60.776 16.043 1.000 33.98 ATOM 7664 O HOH 486 78.365 30.500 32.549 1.000 39.62 ATOM 7665 O HOH 487 115.947 27.013 6.468 1.000 35.66 ATOM 7666 O HOH 488 102.897 41.478 35.832 1.000 37.34 ATOM 7667 O HOH 489 84.341 57.813 34.619 1.000 29.69 ATOM 7668 O HOH 490 100.125 3.494 19.130 1.000 26.61 ATOM 7669 O HOH 491 50.809 20.138 18.682 1.000 52.18 ATOM 7670 O HOH 492 86.185 28.643 28.091 1.000 42.40 ATOM 7671 O HOH 493 99.822 58.547 9.222 1.000 35.54 ATOM 7672 O HOH 494 78.317 33.116 28.899 1.000 33.46 ATOM 7673 O HOH 495 83.739 18.024 36.847 1.000 33.56 ATOM 7674 O HOH 496 75.125 59.664 10.426 1.000 32.84 ATOM 7675 O HOH 497 76.115 31.609 28.684 1.000 24.76 ATOM 7676 O HOH 498 77.499 24.626 24.992 1.000 24.37 ATOM 7677 O HOH 499 92.431 54.586 37.374 1.000 32.36 ATOM 7678 O HOH 500 67.858 50.628 47.734 1.000 30.18 ATOM 7679 O HOH 501 98.318 1.761 23.333 1.000 30.71 ATOM 7680 O HOH 502 72.986 15.557 47.384 1.000 34.73 ATOM 7681 O HOH 503 68.995 54.791 36.757 1.000 31.47 ATOM 7682 O HOH 504 101.723 41.946 18.346 1.000 30.00 ATOM 7683 O HOH 505 82.264 34.952 23.539 1.000 25.17 ATOM 7684 O HOH 506 56.697 47.408 25.618 1.000 31.14 ATOM 7685 O HOH 507 87.847 28.731 25.957 1.000 28.11 ATOM 7686 O HOH 508 95.244 10.416 8.064 1.000 32.16 ATOM 7687 O HOH 509 56.627 19.004 18.253 1.000 26.24 ATOM 7688 O HOH 510 57.854 45.037 24.642 1.000 36.65 ATOM 7689 O HOH 511 78.741 32.690 33.128 1.000 29.92 ATOM 7690 O HOH 512 104.124 6.696 9.404 1.000 27.70 ATOM 7691 O HOH 513 116.359 9.727 16.189 1.000 34.95 ATOM 7692 O HOH 514 49.109 30.125 27.987 1.000 33.92 ATOM 7693 O HOH 515 73.757 37.904 52.165 1.000 34.57 ATOM 7694 O HOH 516 83.597 64.886 14.692 1.000 36.49 ATOM 7695 O HOH 517 55.248 17.298 19.521 1.000 37.21 ATOM 7696 O HOH 518 54.874 22.157 16.029 1.000 45.14 ATOM 7697 O HOH 519 66.187 58.150 19.372 1.000 42.85 ATOM 7698 O HOH 520 72.069 57.310 32.850 1.000 29.22 ATOM 7699 O HOH 521 99.114 18.960 37.026 1.000 33.10 ATOM 7700 O HOH 522 59.194 14.762 9.954 1.000 51.08 ATOM 7701 O HOH 523 96.552 27.459 39.703 1.000 47.86 ATOM 7702 O HOH 524 67.085 25.696 9.189 1.000 47.80 ATOM 7703 O HOH 525 101.022 43.581 7.126 1.000 37.40 ATOM 7704 O HOH 526 78.966 23.519 21.132 1.000 27.15 ATOM 7705 O HOH 527 96.487 2.281 30.380 1.000 32.71 ATOM 7706 O HOH 528 84.740 37.917 45.393 1.000 28.40 ATOM 7707 O HOH 529 98.413 2.783 25.894 1.000 39.61 ATOM 7708 O HOH 530 82.799 55.750 1.882 1.000 43.02 ATOM 7709 O HOH 531 96.924 23.856 37.478 1.000 29.70 ATOM 7710 O HOH 532 105.207 57.177 15.684 1.000 33.51 ATOM 7711 O HOH 533 50.454 48.206 49.545 1.000 47.69 ATOM 7712 O HOH 534 104.933 47.130 24.713 1.000 40.72 ATOM 7713 O HOH 535 110.866 10.401 21.494 1.000 37.91 ATOM 7714 O HOH 536 92.838 24.232 42.078 1.000 41.89 ATOM 7715 O HOH 537 67.555 24.966 46.015 1.000 29.13 ATOM 7716 O HOH 538 78.053 36.477 22.849 1.000 47.09 ATOM 7717 O HOH 539 112.925 12.201 22.087 1.000 37.50 ATOM 7718 O HOH 540 50.757 35.007 25.917 1.000 33.90 ATOM 7719 O HOH 541 68.640 −1.430 15.611 1.000 48.67 ATOM 7720 O HOH 542 51.543 45.251 27.533 1.000 26.17 ATOM 7721 O HOH 543 58.896 50.709 28.085 1.000 37.22 ATOM 7722 O HOH 544 84.790 47.138 1.717 1.000 32.58 ATOM 7723 O HOH 545 49.348 51.235 50.952 1.000 61.64 ATOM 7724 O HOH 546 85.811 28.025 23.962 1.000 29.92 ATOM 7725 O HOH 547 57.308 49.674 25.259 1.000 41.81 ATOM 7726 O HOH 548 76.408 21.933 19.985 1.000 32.05 ATOM 7727 O HOH 549 49.802 38.458 25.007 1.000 23.83 ATOM 7728 O HOH 550 53.861 44.618 23.701 1.000 27.79 ATOM 7729 O HOH 551 102.428 18.900 34.815 1.000 32.12 ATOM 7730 O HOH 552 78.711 57.445 12.607 1.000 32.79 ATOM 7731 O HOH 553 99.312 7.498 33.442 1.000 43.12 ATOM 7732 O HOH 554 98.312 66.410 31.867 1.000 58.37 ATOM 7733 O HOH 555 92.039 18.350 40.142 1.000 41.97 ATOM 7734 O HOH 556 79.528 25.044 23.137 1.000 39.55 ATOM 7735 O HOH 557 93.544 44.872 5.133 1.000 33.79 ATOM 7736 O HOH 558 89.336 10.465 52.529 1.000 55.29 ATOM 7737 O HOH 559 83.570 4.908 36.103 1.000 31.60 ATOM 7738 O HOH 560 90.408 2.929 31.118 1.000 47.04 ATOM 7739 O HOH 561 70.523 60.411 20.819 1.000 29.91 ATOM 7740 O HOH 562 64.140 9.753 40.136 1.000 33.59 ATOM 7741 O HOH 563 78.895 34.022 31.118 1.000 41.66 ATOM 7742 O HOH 564 95.467 56.193 35.984 1.000 31.97 ATOM 7743 O HOH 565 59.692 29.845 54.331 1.000 57.27 ATOM 7744 O HOH 566 80.239 −2.789 16.441 1.000 63.02 ATOM 7745 O HOH 567 65.591 55.864 34.198 1.000 42.97 ATOM 7746 O HOH 568 74.992 59.983 27.745 1.000 27.69 ATOM 7747 O HOH 569 86.483 67.882 25.098 1.000 31.30 ATOM 7748 O HOH 570 115.448 11.042 22.216 1.000 43.17 ATOM 7749 O HOH 571 60.226 17.619 34.965 1.000 35.98 ATOM 7750 O HOH 572 54.360 30.727 49.850 1.000 32.70 ATOM 7751 O HOH 573 79.679 2.761 38.548 1.000 28.97 ATOM 7752 O HOH 574 84.928 67.660 11.745 1.000 44.86 ATOM 7753 O HOH 575 42.718 39.055 40.104 1.000 25.99 ATOM 7754 O HOH 576 83.908 26.100 25.540 1.000 36.04 ATOM 7755 O HOH 577 79.031 30.325 46.969 1.000 47.65 ATOM 7756 O HOH 578 75.839 21.026 5.657 1.000 33.97 ATOM 7757 O HOH 579 65.299 −7.114 42.215 1.000 34.12 ATOM 7758 O HOH 580 94.282 20.055 16.879 1.000 32.93 ATOM 7759 O HOH 581 80.726 4.373 35.442 1.000 33.52 ATOM 7760 O HOH 582 58.177 44.900 50.843 1.000 39.41

[0204] All data collection was carried out on an MAR Research (Hamburg, Germany) 345-mm image plate system installed on a Rigaku RU-200B rotating anode x-ray generator equipped with Osmic mirrors (Osmic, Inc., Troy, Mich.) and using an X-stream cryogenic system (obtained from Molecular Structure Corporation, The Woodlands, Tex.). Data from 0.5° oscillations were integrated and scaled using DENZO and SCALEPACK (Otwinowski et al., Methods Enzymology, Vol. 276, pp. 307-326 (1997)). Crystals were mounted in a fiber loop, dipped in mother liquor with 25% glycerol added, and flash-cooled in liquid nitrogen for data collection at 100° K. An initial data set was collected to 2.4 Å resolution, which was used to obtain a molecular replacement solution. The space group was identified as C2, with an ERAB or HADH2 tetramer in the asymmetric unit.

[0205] The structure was determined by molecular replacement using the program EPMR (Kissinger et al., Acta Crystallography, Vol. D55, pp. 484-491 (1999)) with the wild-type protein tetramer as the search model. A solution was obtained with a correlation coefficient of 0.682 (R-factor=0.361) for data between 15 and 4 Å.

[0206] A subsequent data set was collected to a resolution of 2.0 Å., and this data set was used for refinement. Initial refinement was carried out using standard rigid-body, simulated-annealing, positional, and temperature factor refinement protocols in X-PLOR Version 3.1 (Brünger, XPLOR Manual, Version 3.1, Yale University Press, New Haven, Conn. (1992)) with the application of non-crystallographic symmetry (NCS) restraints. The progress of the refinement was monitored by the free R-factor (Brunger, Nature, Vol. 355, pp. 472-475 (1992)) using 5% of the reflections taken from thin resolution shells. The final stages of refinement were performed using SHELX-97 (Sheldrick et al., Methods Enzymology, Vol. 277, pp. 319-344 (1997)). All data from 25.0 to 2.0 Å were used, and a bulk solvent correction was applied. Local NCS restraints were applied throughout the refinement to residues 5-205 and 220-261 of each monomer. X-FIT (McRee, Journal of Molecular Graphics, Vol. 10, pp. 44-46 (1992)) was used for rebuilding and visual analysis of the structural model. Two-hundred eighty-two (282) water molecules were fit using the automatic water fitting procedures in SHELX while monitoring the effect on the free R factor. The final, refined model includes residues 5-261 of each of the four monomers in the asymmetric unit, with one NAD molecule bound to each monomer and an inhibitor molecule bound to three of the monomers. The final crystallographic R-factor was 0.215 (R_(free)=0.265) for all unique data between 25.0 and 2.0 Å resolution. The RMS deviations from target stereochemistry (Engh et al., Acta Crystallography, Vol. A47, pp. 392-400 (1991)) were 0.005 Å for bond lengths and 1.5° for bond angles. All backbone dihedral angles fall in allowed regions of the Ramachandran plot except those for Ala 154, which occurs in a generously allowed region in all four monomers, and which forms a part of the nucleotide-binding pocket. Proline 224 participates in a cis peptide bond.

[0207] E. The ERAB or HADH2 Crystal Structure

[0208] Wild-type ERAB or HADH2 forms a tetramer in solution (He et al. (1998), supra). Likewise, a tetramer occupied the asymmetric unit of the crystal of the C214R mutant ERAB or HADH2. The conformations of the four subunits were essentially identical with the exception of a mobile loop near the substrate-binding site. Each ERAB or HADH2 monomer (FIG. 1) formed a single domain with the overall polypeptide chain topology characteristic of the SDR family of enzymes (Jörnvall et al., Biochemistry, Vol. 34, pp. 6003-6013 (1995)). The entire polypeptide chain of each of the four monomers had clearly defined electron density with the exception of the first five residues of each monomer, which were apparently disordered. ERAB or HADH2 contained a “Rossman fold” dinucleotide-binding motif (Rossman et al., The Enzymes, Academic Press, NY, pp. 61-102 (1975)), comprising a core β-sheet of seven parallel strands sandwiched between two sets of three α-helices.

[0209] Certain important aspects of the chain fold in ERAB or HADH2 arose from two insertions in the wild-type ERAB or HADH2 sequence relative to other members of the SDR family (see FIG. 2). These insertions formed structural elements that extended from opposite ends of each monomer (FIG. 1B). The first insertion residues (102-107) formed a short β hairpin structure (βDE1,βDE2) that extended the enzyme surface on one side of the substrate-binding cleft. This insertion also extended a monomer-monomer interface in the tetramer by contacting helix αE2 of an adjacent subunit. A second insertion (residues 141-146) extended the loop between αE2 and βE. This loop, which had extensive internal hydrogen bonding, did not lie near any active site region in the tetramer, but contacted Phe223 of an adjacent subunit and extends the subunit interface. Although the functional significance of these two structural elements of the protein is unknown, antibodies raised against peptides that encompass these insertion regions block the interaction of ERAB or HADH2 with β-amyloid (Yan et al. (1997), supra).

[0210] A ribbon representation of the ERAB or HADH2 tetramer is shown in FIG. 3. The subunit interactions in the ERAB or HADH2 tetramer closely resembled those in the tetramers formed by certain other members of the SDR family, including 3α, 20β-hydroxysteroid dehydrogenase [Ghosh et al., Proceedings of National Academy of Science, USA, Vol. 88, pp. 10064-10068 (1991)] and 7α-hydroxysteroid dehydrogenase [Tanaka et al., Biochemistry, Vol. 35, pp. 7715-7730 (1996)]. The subunits in the tetramer were related by three mutually perpendicular two-fold axes, and each subunit contacted each of the other three subunits. The four active site regions were exposed on the outside of the tetramer, with a distance of about 31 Å between the reactive C4 atoms in the nicotinamide ring of each bound NAD⁺ cofactor.

[0211] Electron density for the bound NAD⁺ was clearly visible in all four subunits. Electron density for the inhibitor Compound I, however, was seen in only three of the four monomers in the asymmetric unit. The fourth monomer was involved in a crystal packing interaction that appeared to alter the conformation of the loop formed by residues 205 to 220, which formed one side of the substrate-binding cavity in the enzyme. The binding cleft was narrowed slightly in this monomer, which apparently precluded inhibitor binding. Therefore crystal formation and occupation of the fourth binding site by the inhibitor may be mutually exclusive.

[0212] Conversely, the corresponding region in other members of the SDR family has been observed to be mobile. In 7α-hydroxysteroid dehydrogenase, this region undergoes a large conformational change upon substrate binding (Tanaka et al. (1996) supra). The same region in Drosophila alcohol dehydrogenase is disordered in the enzyme-NAD⁺ complex and assumes differing conformations in the presence of different bound inhibitors (Benach et al., Journal of Molecular Biology, Vol. 289, No. 2, pp. 335-55 (1999)). In the crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase, this region is also observed to be disordered in the absence of substrate (Hülsmeyer et al., Protein Science, Vol. 7, pp. 1286-1293 (1998)). The flexibility of the substrate-binding flap may be important in allowing these enzymes to accommodate multiple substrates.

[0213] In the presence of inhibitor Compound I, the substrate-binding cavity formed a long, narrow cleft. One side of the cleft was composed of residues from two strands of the protein (residues 95-99 and 155-168). Residues 205-217, which formed part of the flexible substrate-binding flap, formed the other side of the cleft. Residue 214, which was mutated from Cys to Arg to facilitate crystallization, lay within this region but projected toward the exterior of the protein away from the substrate-binding cleft and was not in proximity to the bound inhibitor. The floor of the cleft was formed by the carboxy-terminus of the protein (residues 257-261). The substrate-binding cleft was largely hydrophobic in nature. A series of lysine residues (Lys 99, Lys 104, Lys 105) lay outside of the cleft at the site of the β-hairpin insertion region. These residues lay about 20 to 30 Å away from the reactive C4 atom of the NAD⁺, which corresponded to the distance between the phosphates and the reactive carbonyl group in an extended acetoacetyl-CoA molecule. This insertion in ERAB or HADH2 may therefore contribute to the affinity of the enzyme for acetoacetyl-CoA as a substrate.

[0214] While the invention has been described in conjunction with examples and preferred embodiments thereof, it is to be understood that the foregoing description is exemplary and explanatory in nature, and is intended to illustrate the invention and its preferred embodiments. Thus, the invention is intended to be defined not by the above description, but by the following claims and their equivalents.

1 24 1 786 DNA Homo sapiens full length mutant ERAB C214R 1 atggcagcag cgtgtcggag cgtgaagggc ctggtggcgg taataaccgg aggagcctcg 60 ggcctgggcc tggccacggc ggagcgactt gtggggcagg gagcctctgc tgtgcttctg 120 gacctgccca actcgggtgg ggaggcccaa gccaagaagt taggaaacaa ctgcgttttc 180 gccccagccg acgtgacctc tgagaaggat gtgcaaacag ctctggctct agcaaaagga 240 aagtttggcc gtgtggatgt agctgtcaac tgtgcaggca tcgcggtggc tagcaagacg 300 tacaacttaa agaagggcca gacccatacc ttggaagact tccagcgagt tcttgatgtg 360 aatctcatgg gcaccttcaa tgtgatccgc ctggtggctg gtgagatggg ccagaatgaa 420 ccagaccagg gaggccaacg tggggtcatc atcaacactg ccagtgtggc tgccttcgag 480 ggtcaggttg gacaagctgc atactctgct tccaaggggg gaatagtggg catgacactg 540 cccattgctc gggatctggc tcccataggt atccgggtga tgaccattgc cccaggtctg 600 tttggcaccc cactgctgac cagcctccca gagaaagtgc gtaacttctt agccagccaa 660 gtgcccttcc ctagccgact gggtgaccct gctgagtatg ctcacctcgt acaggccatc 720 atcgagaacc cattcctcaa tggagaggtc atccggctgg atggggctat tcgtatgcag 780 ccttaa 786 2 261 PRT Homo sapiens full length mutant ERAB C214R 2 Met Ala Ala Ala Cys Arg Ser Val Lys Gly Leu Val Ala Val Ile Thr 1 5 10 15 Gly Gly Ala Ser Gly Leu Gly Leu Ala Thr Ala Glu Arg Leu Val Gly 20 25 30 Gln Gly Ala Ser Ala Val Leu Leu Asp Leu Pro Asn Ser Gly Gly Glu 35 40 45 Ala Gln Ala Lys Lys Leu Gly Asn Asn Cys Val Phe Ala Pro Ala Asp 50 55 60 Val Thr Ser Glu Lys Asp Val Gln Thr Ala Leu Ala Leu Ala Lys Gly 65 70 75 80 Lys Phe Gly Arg Val Asp Val Ala Val Asn Cys Ala Gly Ile Ala Val 85 90 95 Ala Ser Lys Thr Tyr Asn Leu Lys Lys Gly Gln Thr His Thr Leu Glu 100 105 110 Asp Phe Gln Arg Val Leu Asp Val Asn Leu Met Gly Thr Phe Asn Val 115 120 125 Ile Arg Leu Val Ala Gly Glu Met Gly Gln Asn Glu Pro Asp Gln Gly 130 135 140 Gly Gln Arg Gly Val Ile Ile Asn Thr Ala Ser Val Ala Ala Phe Glu 145 150 155 160 Gly Gln Val Gly Gln Ala Ala Tyr Ser Ala Ser Lys Gly Gly Ile Val 165 170 175 Gly Met Thr Leu Pro Ile Ala Arg Asp Leu Ala Pro Ile Gly Ile Arg 180 185 190 Val Met Thr Ile Ala Pro Gly Leu Phe Gly Thr Pro Leu Leu Thr Ser 195 200 205 Leu Pro Glu Lys Val Arg Asn Phe Leu Ala Ser Gln Val Pro Phe Pro 210 215 220 Ser Arg Leu Gly Asp Pro Ala Glu Tyr Ala His Leu Val Gln Ala Ile 225 230 235 240 Ile Glu Asn Pro Phe Leu Asn Gly Glu Val Ile Arg Leu Asp Gly Ala 245 250 255 Ile Arg Met Gln Pro 260 3 786 DNA Homo sapiens full length mutant ERAB C5V 3 atggcagcag ctgttcggag cgtgaagggc ctggtggcgg taataaccgg aggagcctcg 60 ggcctgggcc tggccacggc ggagcgactt gtggggcagg gagcctctgc tgtgcttctg 120 gacctgccca actcgggtgg ggaggcccaa gccaagaagt taggaaacaa ctgcgttttc 180 gccccagccg acgtgacctc tgagaaggat gtgcaaacag ctctggctct agcaaaagga 240 aagtttggcc gtgtggatgt agctgtcaac tgtgcaggca tcgcggtggc tagcaagacg 300 tacaacttaa agaagggcca gacccatacc ttggaagact tccagcgagt tcttgatgtg 360 aatctcatgg gcaccttcaa tgtgatccgc ctggtggctg gtgagatggg ccagaatgaa 420 ccagaccagg gaggccaacg tggggtcatc atcaacactg ccagtgtggc tgccttcgag 480 ggtcaggttg gacaagctgc atactctgct tccaaggggg gaatagtggg catgacactg 540 cccattgctc gggatctggc tcccataggt atccgggtga tgaccattgc cccaggtctg 600 tttggcaccc cactgctgac cagcctccca gagaaagtgt gcaacttctt ggccagccaa 660 gtgcccttcc ctagccgact gggtgaccct gctgagtatg ctcacctcgt acaggccatc 720 atcgagaacc cattcctcaa tggagaggtc atccggctgg atggggctat tcgtatgcag 780 ccttaa 786 4 261 PRT Homo sapiens full length mutant ERAB C5V 4 Met Ala Ala Ala Val Arg Ser Val Lys Gly Leu Val Ala Val Ile Thr 1 5 10 15 Gly Gly Ala Ser Gly Leu Gly Leu Ala Thr Ala Glu Arg Leu Val Gly 20 25 30 Gln Gly Ala Ser Ala Val Leu Leu Asp Leu Pro Asn Ser Gly Gly Glu 35 40 45 Ala Gln Ala Lys Lys Leu Gly Asn Asn Cys Val Phe Ala Pro Ala Asp 50 55 60 Val Thr Ser Glu Lys Asp Val Gln Thr Ala Leu Ala Leu Ala Lys Gly 65 70 75 80 Lys Phe Gly Arg Val Asp Val Ala Val Asn Cys Ala Gly Ile Ala Val 85 90 95 Ala Ser Lys Thr Tyr Asn Leu Lys Lys Gly Gln Thr His Thr Leu Glu 100 105 110 Asp Phe Gln Arg Val Leu Asp Val Asn Leu Met Gly Thr Phe Asn Val 115 120 125 Ile Arg Leu Val Ala Gly Glu Met Gly Gln Asn Glu Pro Asp Gln Gly 130 135 140 Gly Gln Arg Gly Val Ile Ile Asn Thr Ala Ser Val Ala Ala Phe Glu 145 150 155 160 Gly Gln Val Gly Gln Ala Ala Tyr Ser Ala Ser Lys Gly Gly Ile Val 165 170 175 Gly Met Thr Leu Pro Ile Ala Arg Asp Leu Ala Pro Ile Gly Ile Arg 180 185 190 Val Met Thr Ile Ala Pro Gly Leu Phe Gly Thr Pro Leu Leu Thr Ser 195 200 205 Leu Pro Glu Lys Val Cys Asn Phe Leu Ala Ser Gln Val Pro Phe Pro 210 215 220 Ser Arg Leu Gly Asp Pro Ala Glu Tyr Ala His Leu Val Gln Ala Ile 225 230 235 240 Ile Glu Asn Pro Phe Leu Asn Gly Glu Val Ile Arg Leu Asp Gly Ala 245 250 255 Ile Arg Met Gln Pro 260 5 786 DNA Homo sapiens full length mutant ERAB C58V 5 atggcagcag cgtgtcggag cgtgaagggc ctggtggcgg taataaccgg aggagcctcg 60 ggcctgggcc tggccacggc ggagcgactt gtggggcagg gagcctctgc tgtgcttctg 120 gacctgccca actcgggtgg ggaggcccaa gccaagaagt taggaaacaa cgttgttttc 180 gccccagccg acgtgacctc tgagaaggat gtgcaaacag ctctggctct agcaaaagga 240 aagtttggcc gtgtggatgt agctgtcaac tgtgcaggca tcgcggtggc tagcaagacg 300 tacaacttaa agaagggcca gacccatacc ttggaagact tccagcgagt tcttgatgtg 360 aatctcatgg gcaccttcaa tgtgatccgc ctggtggctg gtgagatggg ccagaatgaa 420 ccagaccagg gaggccaacg tggggtcatc atcaacactg ccagtgtggc tgccttcgag 480 ggtcaggttg gacaagctgc atactctgct tccaaggggg gaatagtggg catgacactg 540 cccattgctc gggatctggc tcccataggt atccgggtga tgaccattgc cccaggtctg 600 tttggcaccc cactgctgac cagcctccca gagaaagtgt gcaacttctt ggccagccaa 660 gtgcccttcc ctagccgact gggtgaccct gctgagtatg ctcacctcgt acaggccatc 720 atcgagaacc cattcctcaa tggagaggtc atccggctgg atggggctat tcgtatgcag 780 ccttaa 786 6 261 PRT Homo sapiens full length mutant ERAB C58V 6 Met Ala Ala Ala Cys Arg Ser Val Lys Gly Leu Val Ala Val Ile Thr 1 5 10 15 Gly Gly Ala Ser Gly Leu Gly Leu Ala Thr Ala Glu Arg Leu Val Gly 20 25 30 Gln Gly Ala Ser Ala Val Leu Leu Asp Leu Pro Asn Ser Gly Gly Glu 35 40 45 Ala Gln Ala Lys Lys Leu Gly Asn Asn Val Val Phe Ala Pro Ala Asp 50 55 60 Val Thr Ser Glu Lys Asp Val Gln Thr Ala Leu Ala Leu Ala Lys Gly 65 70 75 80 Lys Phe Gly Arg Val Asp Val Ala Val Asn Cys Ala Gly Ile Ala Val 85 90 95 Ala Ser Lys Thr Tyr Asn Leu Lys Lys Gly Gln Thr His Thr Leu Glu 100 105 110 Asp Phe Gln Arg Val Leu Asp Val Asn Leu Met Gly Thr Phe Asn Val 115 120 125 Ile Arg Leu Val Ala Gly Glu Met Gly Gln Asn Glu Pro Asp Gln Gly 130 135 140 Gly Gln Arg Gly Val Ile Ile Asn Thr Ala Ser Val Ala Ala Phe Glu 145 150 155 160 Gly Gln Val Gly Gln Ala Ala Tyr Ser Ala Ser Lys Gly Gly Ile Val 165 170 175 Gly Met Thr Leu Pro Ile Ala Arg Asp Leu Ala Pro Ile Gly Ile Arg 180 185 190 Val Met Thr Ile Ala Pro Gly Leu Phe Gly Thr Pro Leu Leu Thr Ser 195 200 205 Leu Pro Glu Lys Val Cys Asn Phe Leu Ala Ser Gln Val Pro Phe Pro 210 215 220 Ser Arg Leu Gly Asp Pro Ala Glu Tyr Ala His Leu Val Gln Ala Ile 225 230 235 240 Ile Glu Asn Pro Phe Leu Asn Gly Glu Val Ile Arg Leu Asp Gly Ala 245 250 255 Ile Arg Met Gln Pro 260 7 786 DNA Homo sapiens wild type ERAB 7 atggcagcag cgtgtcggag cgtgaagggc ctggtggcgg taataaccgg aggagcctcg 60 ggcctgggcc tggccacggc ggagcgactt gtggggcagg gagcctctgc tgtgcttctg 120 gacctgccca actcgggtgg ggaggcccaa gccaagaagt taggaaacaa ctgcgttttc 180 gccccagccg acgtgacctc tgagaaggat gtgcaaacag ctctggctct agcaaaagga 240 aagtttggcc gtgtggatgt agctgtcaac tgtgcaggca tcgcggtggc tagcaagacg 300 tacaacttaa agaagggcca gacccatacc ttggaagact tccagcgagt tcttgatgtg 360 aatctcatgg gcaccttcaa tgtgatccgc ctggtggctg gtgagatggg ccagaatgaa 420 ccagaccagg gaggccaacg tggggtcatc atcaacactg ccagtgtggc tgccttcgag 480 ggtcaggttg gacaagctgc atactctgct tccaaggggg gaatagtggg catgacactg 540 cccattgctc gggatctggc tcccataggt atccgggtga tgaccattgc cccaggtctg 600 tttggcaccc cactgctgac cagcctccca gagaaagtgt gcaacttctt ggccagccaa 660 gtgcccttcc ctagccgact gggtgaccct gctgagtatg ctcacctcgt acaggccatc 720 atcgagaacc cattcctcaa tggagaggtc atccggctgg atggggctat tcgtatgcag 780 ccttaa 786 8 261 PRT Homo sapiens wild type ERAB 8 Met Ala Ala Ala Cys Arg Ser Val Lys Gly Leu Val Ala Val Ile Thr 1 5 10 15 Gly Gly Ala Ser Gly Leu Gly Leu Ala Thr Ala Glu Arg Leu Val Gly 20 25 30 Gln Gly Ala Ser Ala Val Leu Leu Asp Leu Pro Asn Ser Gly Gly Glu 35 40 45 Ala Gln Ala Lys Lys Leu Gly Asn Asn Cys Val Phe Ala Pro Ala Asp 50 55 60 Val Thr Ser Glu Lys Asp Val Gln Thr Ala Leu Ala Leu Ala Lys Gly 65 70 75 80 Lys Phe Gly Arg Val Asp Val Ala Val Asn Cys Ala Gly Ile Ala Val 85 90 95 Ala Ser Lys Thr Tyr Asn Leu Lys Lys Gly Gln Thr His Thr Leu Glu 100 105 110 Asp Phe Gln Arg Val Leu Asp Val Asn Leu Met Gly Thr Phe Asn Val 115 120 125 Ile Arg Leu Val Ala Gly Glu Met Gly Gln Asn Glu Pro Asp Gln Gly 130 135 140 Gly Gln Arg Gly Val Ile Ile Asn Thr Ala Ser Val Ala Ala Phe Glu 145 150 155 160 Gly Gln Val Gly Gln Ala Ala Tyr Ser Ala Ser Lys Gly Gly Ile Val 165 170 175 Gly Met Thr Leu Pro Ile Ala Arg Asp Leu Ala Pro Ile Gly Ile Arg 180 185 190 Val Met Thr Ile Ala Pro Gly Leu Phe Gly Thr Pro Leu Leu Thr Ser 195 200 205 Leu Pro Glu Lys Val Cys Asn Phe Leu Ala Ser Gln Val Pro Phe Pro 210 215 220 Ser Arg Leu Gly Asp Pro Ala Glu Tyr Ala His Leu Val Gln Ala Ile 225 230 235 240 Ile Glu Asn Pro Phe Leu Asn Gly Glu Val Ile Arg Leu Asp Gly Ala 245 250 255 Ile Arg Met Gln Pro 260 9 37 DNA Artificial Sequence Description of Artificial Sequence PCR Primer 9 gggcacacca tggcagcagc gtgtcggagc gtgaagg 37 10 40 DNA Artificial Sequence Description of Artificial Sequence PCR Primer 10 agctttcggc cgttaaggct gcatacgaat agccccatcc 40 11 30 DNA Artificial Sequence Description of Artificial Sequence Oligonucleotide for C5V 11 ccatggcagc agctgttcgg agcgtgaagg 30 12 34 DNA Artificial Sequence Description of Artificial Sequence Oligonucleotide for C58V 12 gaagttagga aacaacgttg ttttcgcccc agcc 34 13 34 DNA Artificial Sequence Description of Artificial Sequence Oligonucleotide for C214R 13 ccagagaaag tgcgtaactt cttagccagc caag 34 14 255 PRT Escherichia coli 14 Met Phe Asn Ser Asp Asn Leu Arg Leu Asp Gly Lys Cys Ala Ile Ile 1 5 10 15 Thr Gly Ala Gly Ala Gly Ile Gly Lys Glu Ile Ala Ile Thr Phe Ala 20 25 30 Thr Ala Gly Ala Ser Val Val Val Ser Asp Ile Asn Ala Asp Ala Ala 35 40 45 Asn His Val Val Asp Glu Ile Gln Gln Leu Gly Gly Gln Ala Phe Ala 50 55 60 Cys Arg Cys Asp Ile Thr Ser Glu Gln Glu Leu Ser Ala Leu Ala Asp 65 70 75 80 Phe Ala Ile Ser Lys Leu Gly Lys Val Asp Ile Leu Val Asn Asn Ala 85 90 95 Gly Gly Gly Gly Pro Lys Pro Phe Asp Met Pro Met Ala Asp Phe Arg 100 105 110 Arg Ala Tyr Glu Leu Asn Val Phe Ser Phe Phe His Leu Ser Gln Leu 115 120 125 Val Ala Pro Glu Met Glu Lys Asn Gly Gly Gly Val Ile Leu Thr Ile 130 135 140 Thr Ser Met Ala Ala Glu Asn Lys Asn Ile Asn Met Thr Ser Tyr Ala 145 150 155 160 Ser Ser Lys Ala Ala Ala Ser His Leu Val Arg Asn Met Ala Phe Asp 165 170 175 Leu Gly Glu Lys Asn Ile Arg Val Asn Gly Ile Ala Pro Gly Ala Ile 180 185 190 Leu Thr Asp Ala Leu Lys Ser Val Ile Thr Pro Glu Ile Glu Gln Lys 195 200 205 Met Leu Gln His Thr Pro Ile Arg Arg Leu Gly Gln Pro Gln Asp Ile 210 215 220 Ala Asn Ala Ala Leu Phe Leu Cys Ser Pro Ala Ala Ser Trp Val Ser 225 230 235 240 Gly Gln Ile Leu Thr Val Ser Gly Gly Gly Val Gln Glu Leu Asn 245 250 255 15 253 PRT Steptomyces hydrogenans 15 Asn Asp Leu Ser Gly Lys Thr Val Ile Ile Thr Gly Gly Ala Arg Gly 1 5 10 15 Leu Gly Ala Glu Ala Ala Arg Gln Ala Val Ala Ala Gly Ala Arg Val 20 25 30 Val Leu Ala Asp Val Leu Asp Glu Glu Gly Ala Ala Thr Ala Arg Glu 35 40 45 Leu Gly Asp Ala Ala Arg Tyr Gln His Leu Asp Val Thr Ile Glu Glu 50 55 60 Asp Trp Gln Arg Val Val Ala Tyr Ala Arg Glu Glu Phe Gly Ser Val 65 70 75 80 Asp Gly Leu Val Asn Asn Ala Gly Ile Ser Thr Gly Met Phe Leu Glu 85 90 95 Thr Glu Ser Val Glu Arg Phe Arg Lys Val Val Glu Ile Asn Leu Thr 100 105 110 Gly Val Phe Ile Gly Met Lys Thr Val Ile Pro Ala Met Lys Asp Ala 115 120 125 Gly Gly Gly Ser Ile Val Asn Ile Ser Ser Ala Ala Gly Leu Met Gly 130 135 140 Leu Ala Leu Thr Ser Ser Tyr Gly Ala Ser Lys Trp Gly Val Arg Gly 145 150 155 160 Leu Ser Lys Leu Ala Ala Val Glu Leu Gly Thr Asp Arg Ile Arg Val 165 170 175 Asn Ser Val His Pro Gly Met Thr Tyr Thr Pro Met Thr Ala Glu Thr 180 185 190 Gly Ile Arg Gln Gly Glu Gly Asn Tyr Pro Asn Thr Pro Met Gly Arg 195 200 205 Val Gly Glu Pro Gly Glu Ile Ala Gly Ala Val Val Lys Leu Leu Ser 210 215 220 Asp Thr Ser Ser Tyr Val Thr Gly Ala Glu Leu Ala Val Asp Gly Gly 225 230 235 240 Trp Thr Thr Gly Pro Thr Val Lys Tyr Val Met Gly Gln 245 250 16 274 PRT Homo sapiens 16 Ala Arg Thr Val Val Leu Ile Thr Gly Cys Ser Ser Gly Ile Gly Leu 1 5 10 15 His Leu Ala Val Arg Leu Ala Ser Asp Pro Ser Gln Ser Phe Lys Val 20 25 30 Tyr Ala Thr Leu Arg Asp Leu Lys Thr Gln Gly Arg Leu Trp Glu Ala 35 40 45 Ala Arg Ala Leu Ala Cys Pro Pro Gly Ser Leu Glu Thr Leu Gln Leu 50 55 60 Asp Val Arg Asp Ser Lys Ser Val Ala Ala Ala Arg Glu Arg Val Thr 65 70 75 80 Glu Gly Arg Val Asp Val Leu Val Cys Asn Ala Gly Leu Gly Leu Leu 85 90 95 Gly Pro Leu Glu Ala Leu Gly Glu Asp Ala Val Ala Ser Val Leu Asp 100 105 110 Val Asn Val Val Gly Thr Val Arg Met Leu Gln Ala Phe Leu Pro Asp 115 120 125 Met Lys Arg Arg Gly Ser Gly Arg Val Leu Val Thr Gly Ser Val Gly 130 135 140 Gly Leu Met Gly Leu Pro Phe Asn Asp Val Tyr Cys Ala Ser Lys Phe 145 150 155 160 Ala Leu Glu Gly Leu Cys Glu Ser Leu Ala Val Leu Leu Leu Pro Phe 165 170 175 Gly Val His Leu Ser Leu Ile Glu Cys Gly Pro Val His Thr Ala Phe 180 185 190 Met Glu Lys Val Leu Gly Ser Pro Glu Glu Val Leu Asp Arg Thr Asp 195 200 205 Ile His Thr Phe His Arg Phe Tyr Gln Tyr Leu Ala His Ser Lys Gln 210 215 220 Val Phe Arg Glu Ala Ala Gln Asn Pro Glu Glu Val Ala Glu Val Phe 225 230 235 240 Leu Thr Ala Leu Arg Ala Pro Lys Pro Thr Leu Arg Tyr Phe Thr Thr 245 250 255 Glu Arg Phe Leu Pro Leu Leu Arg Met Arg Leu Asp Asp Pro Ser Gly 260 265 270 Ser Asn 17 259 PRT Homo sapiens 17 Ser Gln Leu Gln Asn Arg Leu Arg Ser Ala Leu Ala Leu Val Thr Gly 1 5 10 15 Ala Gly Ser Gly Ile Gly Arg Ala Val Ser Val Arg Leu Ala Gly Glu 20 25 30 Gly Ala Thr Val Ala Ala Cys Asp Leu Asp Arg Ala Ala Ala Gln Glu 35 40 45 Thr Val Arg Leu Leu Gly Gly Pro Gly Ser Lys Glu Gly Pro Pro Arg 50 55 60 Gly Asn His Ala Ala Phe Gln Ala Asp Val Ser Glu Ala Arg Ala Ala 65 70 75 80 Arg Cys Leu Leu Glu Gln Val Gln Ala Cys Phe Ser Arg Pro Pro Ser 85 90 95 Val Val Val Ser Cys Ala Gly Ile Thr Gln Asp Glu Phe Leu Leu His 100 105 110 Met Ser Glu Asp Asp Trp Asp Lys Val Ile Ala Val Asn Leu Lys Gly 115 120 125 Thr Phe Leu Val Thr Gln Ala Ala Ala Gln Ala Leu Val Ser Asn Gly 130 135 140 Cys Arg Gly Ser Ile Ile Asn Ile Ser Ser Ile Val Gly Lys Val Gly 145 150 155 160 Asn Val Gly Gln Thr Asn Tyr Ala Ala Ser Lys Ala Gly Val Ile Gly 165 170 175 Leu Thr Gln Thr Ala Ala Arg Glu Leu Gly Arg His Gly Ile Arg Cys 180 185 190 Asn Ser Val Leu Pro Gly Phe Ile Ala Thr Pro Met Thr Gln Lys Val 195 200 205 Pro Gln Lys Val Val Asp Lys Ile Thr Glu Met Ile Pro Met Gly His 210 215 220 Leu Gly Asp Pro Glu Asp Val Ala Asp Val Val Ala Phe Leu Ala Ser 225 230 235 240 Glu Asp Ser Gly Tyr Ile Thr Gly Thr Ser Val Glu Val Thr Gly Gly 245 250 255 Leu Phe Met 18 266 PRT Homo sapiens 18 Met His Val Asn Gly Lys Val Ala Leu Val Thr Gly Ala Ala Gln Gly 1 5 10 15 Ile Gly Arg Ala Phe Ala Glu Ala Leu Leu Leu Lys Gly Ala Lys Val 20 25 30 Ala Leu Val Asp Trp Asn Leu Glu Ala Gly Val Gln Cys Lys Ala Ala 35 40 45 Leu Asp Glu Gln Phe Glu Pro Gln Lys Thr Leu Phe Ile Gln Cys Asp 50 55 60 Val Ala Asp Gln Gln Gln Leu Arg Asp Thr Phe Arg Lys Val Val Asp 65 70 75 80 His Phe Gly Arg Leu Asp Ile Leu Val Asn Asn Ala Gly Val Asn Asn 85 90 95 Glu Lys Asn Trp Glu Lys Thr Leu Gln Ile Asn Leu Val Ser Val Ile 100 105 110 Ser Gly Thr Tyr Leu Gly Leu Asp Tyr Met Ser Lys Gln Asn Gly Gly 115 120 125 Glu Gly Gly Ile Ile Ile Asn Met Ser Ser Leu Ala Gly Leu Met Pro 130 135 140 Val Ala Gln Gln Pro Val Tyr Cys Ala Ser Lys His Gly Ile Val Gly 145 150 155 160 Phe Thr Arg Ser Ala Ala Leu Ala Ala Asn Leu Met Asn Ser Gly Val 165 170 175 Arg Leu Asn Ala Ile Cys Pro Gly Phe Val Asn Thr Ala Ile Leu Glu 180 185 190 Ser Ile Glu Lys Glu Glu Asn Met Gly Gln Tyr Ile Glu Tyr Lys Asp 195 200 205 His Ile Lys Asp Met Ile Lys Tyr Tyr Gly Ile Leu Asp Pro Pro Leu 210 215 220 Ile Ala Asn Gly Leu Ile Thr Leu Ile Glu Asp Asp Ala Leu Asn Gly 225 230 235 240 Ala Ile Met Lys Ile Thr Thr Ser Lys Gly Ile His Phe Gln Asp Tyr 245 250 255 Asp Thr Thr Pro Phe Gln Ala Lys Thr Gln 260 265 19 786 DNA Homo sapiens full length mutant ERAB C214A 19 atggcagcag cgtgtcggag cgtgaagggc ctggtggcgg taataaccgg aggagcctcg 60 ggcctgggcc tggccacggc ggagcgactt gtggggcagg gagcctctgc tgtgcttctg 120 gacctgccca actcgggtgg ggaggcccaa gccaagaagt taggaaacaa ctgcgttttc 180 gccccagccg acgtgacctc tgagaaggat gtgcaaacag ctctggctct agcaaaagga 240 aagtttggcc gtgtggatgt agctgtcaac tgtgcaggca tcgcggtggc tagcaagacg 300 tacaacttaa agaagggcca gacccatacc ttggaagact tccagcgagt tcttgatgtg 360 aatctcatgg gcaccttcaa tgtgatccgc ctggtggctg gtgagatggg ccagaatgaa 420 ccagaccagg gaggccaacg tggggtcatc atcaacactg ccagtgtggc tgccttcgag 480 ggtcaggttg gacaagctgc atactctgct tccaaggggg gaatagtggg catgacactg 540 cccattgctc gggatctggc tcccataggt atccgggtga tgaccattgc cccaggtctg 600 tttggcaccc cactgctgac cagcctccca gagaaagtag caaacttcct cgccagccaa 660 gtgcccttcc ctagccgact gggtgaccct gctgagtatg ctcacctcgt acaggccatc 720 atcgagaacc cattcctcaa tggagaggtc atccggctgg atggggctat tcgtatgcag 780 ccttaa 786 20 261 PRT Homo sapiens full length mutant ERAB C214A 20 Met Ala Ala Ala Cys Arg Ser Val Lys Gly Leu Val Ala Val Ile Thr 1 5 10 15 Gly Gly Ala Ser Gly Leu Gly Leu Ala Thr Ala Glu Arg Leu Val Gly 20 25 30 Gln Gly Ala Ser Ala Val Leu Leu Asp Leu Pro Asn Ser Gly Gly Glu 35 40 45 Ala Gln Ala Lys Lys Leu Gly Asn Asn Cys Val Phe Ala Pro Ala Asp 50 55 60 Val Thr Ser Glu Lys Asp Val Gln Thr Ala Leu Ala Leu Ala Lys Gly 65 70 75 80 Lys Phe Gly Arg Val Asp Val Ala Val Asn Cys Ala Gly Ile Ala Val 85 90 95 Ala Ser Lys Thr Tyr Asn Leu Lys Lys Gly Gln Thr His Thr Leu Glu 100 105 110 Asp Phe Gln Arg Val Leu Asp Val Asn Leu Met Gly Thr Phe Asn Val 115 120 125 Ile Arg Leu Val Ala Gly Glu Met Gly Gln Asn Glu Pro Asp Gln Gly 130 135 140 Gly Gln Arg Gly Val Ile Ile Asn Thr Ala Ser Val Ala Ala Phe Glu 145 150 155 160 Gly Gln Val Gly Gln Ala Ala Tyr Ser Ala Ser Lys Gly Gly Ile Val 165 170 175 Gly Met Thr Leu Pro Ile Ala Arg Asp Leu Ala Pro Ile Gly Ile Arg 180 185 190 Val Met Thr Ile Ala Pro Gly Leu Phe Gly Thr Pro Leu Leu Thr Ser 195 200 205 Leu Pro Glu Lys Val Ala Asn Phe Leu Ala Ser Gln Val Pro Phe Pro 210 215 220 Ser Arg Leu Gly Asp Pro Ala Glu Tyr Ala His Leu Val Gln Ala Ile 225 230 235 240 Ile Glu Asn Pro Phe Leu Asn Gly Glu Val Ile Arg Leu Asp Gly Ala 245 250 255 Ile Arg Met Gln Pro 260 21 34 DNA Artificial Sequence Description of Artificial Sequence Oligonucleotide for C214A 21 ccagagaaag tagcaaactt cctcgccagc caag 34 22 786 DNA Homo sapiens full length mutant ERAB C214S 22 atggcagcag cgtgtcggag cgtgaagggc ctggtggcgg taataaccgg aggagcctcg 60 ggcctgggcc tggccacggc ggagcgactt gtggggcagg gagcctctgc tgtgcttctg 120 gacctgccca actcgggtgg ggaggcccaa gccaagaagt taggaaacaa ctgcgttttc 180 gccccagccg acgtgacctc tgagaaggat gtgcaaacag ctctggctct agcaaaagga 240 aagtttggcc gtgtggatgt agctgtcaac tgtgcaggca tcgcggtggc tagcaagacg 300 tacaacttaa agaagggcca gacccatacc ttggaagact tccagcgagt tcttgatgtg 360 aatctcatgg gcaccttcaa tgtgatccgc ctggtggctg gtgagatggg ccagaatgaa 420 ccagaccagg gaggccaacg tggggtcatc atcaacactg ccagtgtggc tgccttcgag 480 ggtcaggttg gacaagctgc atactctgct tccaaggggg gaatagtggg catgacactg 540 cccattgctc gggatctggc tcccataggt atccgggtga tgaccattgc cccaggtctg 600 tttggcaccc cactgctgac cagcctccca gagaaagtgt ctaacttctt agccagccaa 660 gtgcccttcc ctagccgact gggtgaccct gctgagtatg ctcacctcgt acaggccatc 720 atcgagaacc cattcctcaa tggagaggtc atccggctgg atggggctat tcgtatgcag 780 ccttaa 786 23 261 PRT Homo sapiens full length mutant ERAB C214S 23 Met Ala Ala Ala Cys Arg Ser Val Lys Gly Leu Val Ala Val Ile Thr 1 5 10 15 Gly Gly Ala Ser Gly Leu Gly Leu Ala Thr Ala Glu Arg Leu Val Gly 20 25 30 Gln Gly Ala Ser Ala Val Leu Leu Asp Leu Pro Asn Ser Gly Gly Glu 35 40 45 Ala Gln Ala Lys Lys Leu Gly Asn Asn Cys Val Phe Ala Pro Ala Asp 50 55 60 Val Thr Ser Glu Lys Asp Val Gln Thr Ala Leu Ala Leu Ala Lys Gly 65 70 75 80 Lys Phe Gly Arg Val Asp Val Ala Val Asn Cys Ala Gly Ile Ala Val 85 90 95 Ala Ser Lys Thr Tyr Asn Leu Lys Lys Gly Gln Thr His Thr Leu Glu 100 105 110 Asp Phe Gln Arg Val Leu Asp Val Asn Leu Met Gly Thr Phe Asn Val 115 120 125 Ile Arg Leu Val Ala Gly Glu Met Gly Gln Asn Glu Pro Asp Gln Gly 130 135 140 Gly Gln Arg Gly Val Ile Ile Asn Thr Ala Ser Val Ala Ala Phe Glu 145 150 155 160 Gly Gln Val Gly Gln Ala Ala Tyr Ser Ala Ser Lys Gly Gly Ile Val 165 170 175 Gly Met Thr Leu Pro Ile Ala Arg Asp Leu Ala Pro Ile Gly Ile Arg 180 185 190 Val Met Thr Ile Ala Pro Gly Leu Phe Gly Thr Pro Leu Leu Thr Ser 195 200 205 Leu Pro Glu Lys Val Ser Asn Phe Leu Ala Ser Gln Val Pro Phe Pro 210 215 220 Ser Arg Leu Gly Asp Pro Ala Glu Tyr Ala His Leu Val Gln Ala Ile 225 230 235 240 Ile Glu Asn Pro Phe Leu Asn Gly Glu Val Ile Arg Leu Asp Gly Ala 245 250 255 Ile Arg Met Gln Pro 260 24 34 DNA Artificial Sequence Description of Artificial Sequence Oligonucleotide for C214S 24 ccagagaaag tgtctaactt cttagccagc caag 34 

What is claimed is:
 1. An isolated, purified polynucleotide that encodes a mutant Endoplasmic reticulum-associated amyloid β-peptide-binding protein (ERAB) or L-3 -hydroxyacryl-CoA dehydrogenase Type II (HADH2) peptide, wherein said peptide is engineered to avoid cysteine oxidation.
 2. The polynucleotide of claim 1, wherein said polynucleotide encodes an ERAB or HADH2 peptide which has an amino acid other than cysteine at one or all of positions 5, 58, and/or 214 of SEQ ID NO:
 8. 3. An isolated mutant ERAB or HADH2 peptide which is engineered to avoid cysteine oxidation.
 4. The peptide of claim 3 which has an amino acid other than cysteine at one or all of positions 5, 58, and/or 214 of SEQ ID NO:
 8. 5. A crystal structure of a mutant ERAB or HADH2 peptide wherein said peptide is engineered to avoid cysteine oxidation.
 6. The crystal structure of claim 5, wherein said peptide has an amino acid other than cysteine at one or all of positions 5, 58, and/or 214 of SEQ ID NO:
 8. 7. An isolated polynucleotide that encodes a mutant ERAB or HADH2 peptide, wherein said polynucleotide is selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19, and SEQ ID NO: 22, and functional variants thereof.
 8. An isolated polynucleotide that encodes a mutant ERAB or HADH2 peptide, wherein said peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23, and functional variants thereof.
 9. A crystal structure of a mutant ERAB or HADH2 peptide, wherein said peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23, and fragments or variants thereof.
 10. The crystal structure of claim 9, wherein said mutant peptide has an amino acid sequence of SEQ ID NO: 2, or fragments or variants thereof.
 11. The crystal structure of claim 9, wherein said mutant peptide has an amino acid sequence of SEQ ID NO: 4, or fragments or variants thereof.
 12. The crystal structure of claim 9, wherein said mutant peptide has an amino acid sequence of SEQ ID NO: 6, or fragments or variants thereof.
 13. The crystal structure of claim 9, wherein said mutant peptide has an amino acid sequence of SEQ ID NO: 20, or fragments or variants thereof.
 14. The crystal structure of claim 9, wherein said mutant peptide has an amino acid sequence of SEQ ID NO: 23, or fragments or variants thereof.
 15. The crystal structure of claim 5, 6 or 9, wherein said crystal diffracts x-rays at a resolution value of ≦3 Å.
 16. The crystal structure of claim 5, 6 or 9, wherein said crystal diffracts x-rays at a resolution value of ≦2 Å.
 17. The crystal structure of claim 5, 6, or 9, wherein said crystal peptide mutant is tetrameric.
 18. A crystal structure of a mutant ERAB or HADH2 peptide:ligand:NAD⁺ complex wherein said peptide is engineered to avoid cysteine oxidation.
 19. The crystal structure of claim 18, wherein said peptide has an amino acid other than cysteine at one or all of positions 5, 58, and/or 214 of SEQ ID NO:
 8. 20. A crystal structure of a mutant ERAB or HADH2 peptide:ligand:NAD⁺ complex, wherein said peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23, and functional variants thereof.
 21. The crystal structure of claim 18, 19 or 20, wherein the crystal diffracts X-rays for the determination of the atomic coordinates of the complex to a resolution of greater than 3.0 Å.
 22. The crystal structure of claim 20 having the crystal coordinates shown in Table II.
 23. The crystal structure of claim 18, 19 or 20, wherein said ligand is an ERAB or HADH2 inhibitor.
 24. The crystal structure of claim 18, 19 or 20, wherein said ERAB or HADH2 inhibitor is a compound of the formula:


25. An isolated, purified peptide comprising a mutant ERAB or HADH2 peptide, wherein said mutant peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23, and functional variants thereof.
 26. The peptide of claim 25 having an amino acid sequence comprising amino acids 90 to 261 of SEQ ID NO: 2 or functional variants thereof.
 27. An isolated, purified ERAB or HADH2 peptide comprising a fold, wherein said fold comprises: a core β-sheet of seven strands sandwiched between two sets of three α-helices; and first and second insert domains, relative to other members of the short-chain dehydrogenase/reductase (SDR) family, the first insert domain forming a β hairpin that extends the surface of said ERAB or HADH2 peptide on one side of a substrate-binding cleft, and the second insert domain extending a loop between an α-helix and a β-sheet, wherein said α-helix comprises amino acid residues having a sequence of amino acid 123-136 of SEQ ID NO: 2, and said β-sheet comprises amino acid residues having a sequence of amino acid 148-153 of SEQ ID NO:
 2. 28. An isolated, purified mutant ERAB or HADH2 peptide comprising a fold, wherein said fold comprises: a core β-sheet of seven strands sandwiched between two sets of three α-helices; and first and second insert domains, relative to other members of the short-chain dehydrogenase/reductase (SDR) family, the first insert domain forming a β hairpin that extends the surface of said ERAB or HADH2 peptide on one side of a substrate-binding cleft, and the second insert domain extending a loop between an α-helix and a β-sheet, wherein said peptide is engineered to avoid cysteine oxidation.
 29. The peptide of claim 28, wherein said peptide has an amino acid other than cysteine at one or all of positions 5, 58, and/or 214 of SEQ ID NO:
 8. 30. The peptide according to claim 28, wherein said α-helix comprises amino acid residues having a sequence of amino acid 123-136 of SEQ ID NO: 2 and said β-sheet comprises amino acid residues having a sequence of amino acid 148-153 of SEQ ID NO: 2, and further comprises a substrate-binding site involving residues selected from the group consisting of (a) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO. 2; (b) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 4; (c) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 6; (d) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 20; and (e) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO:
 23. 31. An isolated, purified mutant ERAB or HADH2 peptide comprising a fold, wherein said fold comprises: a core β-sheet of seven strands sandwiched between two sets of three α-helices; and first and second insert domains, relative to other members of the short-chain dehydrogenase/reductase (SDR) family, the first insert domain forming a β hairpin that extends the surface of said ERAB or HADH2 peptide on one side of a substrate-binding cleft, and the second insert domain extending a loop between an α-helix comprising residues 123-136 and a β-sheet comprising residues 148-153 of SEQ ID NO:
 2. 32. The peptide according to claim 27, 28 or 31, further comprising a substrate-binding site involving residues selected from the group consisting of (a) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 2; (b) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 4; (c) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 6; (d) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 20; and (e) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO:
 23. 33. The peptide according to claim 31, wherein said first insert domain is at residues 102-107 of SEQ ID NO:
 2. 34. The peptide according to claim 31, wherein said second insert domain is at residues 141-146 of SEQ ID NO:
 2. 35. The peptide according to claim 31, wherein said ERAB or HADH2 is in the form of monomer.
 36. The peptide according to claim 35, wherein said ERAB or HADH2 monomer forms a tetramer when crystallized.
 37. The peptide according to claim 36, further comprising an ERAB or HADH2 cofactor-binding site.
 38. The peptide according to claim 37, wherein said ERAB or HADH2 cofactor is NAD⁺.
 39. An expression vector for producing a mutant ERAB or HADH2 peptide in a host cell, which vector comprises: a polynucleotide that encodes a mutant ERAB or HADH2 peptide, wherein said polynucleotide is the polynucleotide of claim 1, 2, or 7, or functional variants thereof, transcriptional regulatory sequences functional in said host cell operably linked to said polynucleotide; and a selectable marker.
 40. The vector of claim 39, wherein said polynucleotide is selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19, and SEQ ID NO: 22, and functional variants thereof.
 41. A host cell stably transfected and transformed with the polynucleotide that encodes a mutant ERAB or HADH2 peptide, wherein said polynucleotide is the polynucleotide of claim 1, 2, or 7, or functional variants thereof.
 42. The host cell of claim 41, wherein said polynucleotide is selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19, and SEQ ID NO: 22, and functional variants thereof.
 43. A method for identifying a candidate compound for its ability to interact with the human ERAB or HADH2 peptide comprising: (a) expressing an isolated polynucleotide sequence which encodes a mutant ERAB or HADH2 peptide in a host cell capable of producing said peptide, wherein said polynucleotide is the polynucleotide of claim 1, 2, or 7, or functional variants thereof; (b) exposing said mutant ERAB or HADH2 peptide to said candidate compound; and (c) evaluating the interaction of said mutant ERAB or HADH2 peptide with said candidate compound.
 44. The method of claim 43, wherein said polynucleotide is selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 19 and SEQ ID NO: 22, and functional variants thereof.
 45. The method of claim 43, wherein said evaluation step comprises conducting said x-ray crystallography on said ERAB or HADH2 peptide.
 46. The method of claim 45, wherein the results of said x-ray crystallography step are used to determine the three-dimensional molecular structure of the configuration of the ERAB or HADH2 peptide and the binding pockets thereof.
 47. A process of drug design for compounds which interact with an ERAB or HADH2 peptide comprising: (a) crystallizing a mutant ERAB or HADH2 peptide, said peptide being a peptide of claim 3, 4, or 25, or functional variants thereof; (b) resolving the x-ray crystallography of said peptide; (c) applying the data, or a portion thereof, generated from resolving the x-ray crystallography of said peptide to a computer algorithm which generates a model of a three-dimensional structure, said model suitable for use in designing molecules that will interact with said peptide; and (d) applying an interative process whereby various molecular structures are applied to said computer-generated model to identify the compounds which interact with said peptide.
 48. The method of claim 47, wherein said peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23, and functional variants thereof.
 49. The method of claim 47, wherein said process is utilized to identify inhibitors of an ERAB or HADH2 enzyme, said inhibitors serving as lead compounds for the design of potentially therapeutic compounds for the treatment of diseases or disorders associated with the ERAB or HADH2 action.
 50. A method of assessing compounds which are agonists or antagonists of the activity of the human ERAB or HADH2 enzyme comprising: (a) crystallizing a mutant ERAB or HADH2 peptide, said peptide being a peptide of claim 3, 4, or 25, or functional variants thereof; (b) obtaining crystallography coordinates for said crystallized peptide; (c) applying said crystallography coordinates or a portion thereof for said peptide to a computer algorithm such that said algorithm generates a model of a three-dimensional structure, said model suitable for use in designing molecules that will act as agonists or antagonists to said peptide; and (d) applying an iterative process whereby various molecular structures are applied to said computer-generated model to identify potential agonists or antagonists to said peptide.
 51. The method of claim 50, wherein said peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23, and functional variants thereof.
 52. A method of identifying a compound that associates with an ERAB or HADH2 peptide, the method comprising the step of using the crystal coordinates of Table II or a portion thereof to computationally analyze a molecular structure to evaluate a chemical entity for associating with the substrate-binding site of ERAB or HADH2 and identifying those chemical entities that associate with said substrate-binding site, wherein said step of computationally analyzing the molecular structure comprises: (a) storing instructions for processing machine readable data wherein said data comprises crystal coordinates of a mutant ERAB or HADH2 peptide molecule or complex of said peptide, said mutant ERAB or HADH2 peptide being the peptide of claim 3, 4, or 25, or functional variants thereof; and (c) processing said data of crystal coordinates into a three-dimensional structure of said peptide molecule or complex.
 53. The method of claim 52 further comprising the step of displaying said crystal coordinates of the three-dimensional structure.
 54. The method of claim 52, wherein said peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23, and functional variants thereof.
 55. The method of claim 52, wherein said complex is an ERAB or HADH2 peptide:ligand:NAD⁺ complex.
 56. The method of claim 55, wherein said ligand is an ERAB or HADH2 inhibitor.
 57. The method of claim 56, wherein said ligand is a compound of the formula:


58. A method of using a computer processor for analyzing a molecular structure comprising: (a) storing instructions for processing machine readable data wherein said data comprises crystal coordinates of a mutant ERAB or HADH2 peptide molecule or complex of said peptide, said mutant ERAB or HADH2 peptide being the peptide of claim 3, 4, or 25, or functional variants thereof; and (b) processing said data of crystal coordinates into a three-dimensional structure of said peptide molecule or complex.
 59. The method of claim 58 further comprising the step of displaying said crystal coordinates of the three-dimensional structure.
 60. The method of claim 58, wherein said peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20, and SEQ ID NO: 23, and functional variants thereo
 61. The method of claim 58, wherein said complex is an ERAB or HADH2 peptide:ligand:NAD⁺ complex.
 62. The method of claim 61, wherein said ligand is an ERAB or HADH2 inhibitor.
 63. The method of claim 62, wherein said ligand is a compound of the formula:


64. The method of claim 58, wherein said machine readable data storage medium is CD-ROM.
 65. The method of claim 58, wherein said machine readable data storage medium is a magneto-optic disk.
 66. A computer based method for processing X-ray coordinate data into a three-dimensional graphical display of a mutant ERAB or HAHD2 peptide molecule or molecular complex which comprises a substrate binding domain, wherein said mutant ERAB or HADH2 peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 20 and SEQ ID NO: 23, and functional variants thereof.
 67. The method of claim 66, wherein said complex is an ERAB or HADH2 peptide:ligand:NAD⁺ complex.
 68. The method of claim 67, wherein said ligand is an ERAB or HADH2 inhibitor.
 69. The method of claim 66, wherein said X-ray coordinate data is stored in a machine readable storage medium.
 70. The method of claim 66, wherein said three-dimensional graphical display is displayed on a computer monitor.
 71. A crystallized ERAB or HADH2 peptide or an ERAB or HADH2 peptide:cofactor:ligand complex containing a substrate-binding site comprised of amino acid residues selected from the group consisting of (a) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 2; (b) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 4; (c) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 6; (d) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 8; (e) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 20; and (f) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO:
 23. 72. The crystallized peptide or complex of claim 71, wherein said cofactor is NAD⁺.
 73. A method of assessing compounds which are agonists or antagonists of the activity of the human ERAB or HADH2 pepetide comprising: (a) crystallizing an ERAB or HADH2 peptide or ERAB or HADH2 peptide:NAD⁺:ligand complex; (b) obtaining crystallography coordinates for said crystallized peptide or complex; (c) applying said crystallography coordinates or a portion thereof for said peptide to a computer algorithm such that said algorithm generates a model of a substrate-binding site, said model suitable for use in designing molecules that will act as agonists or antagonists to said peptide; and (d) applying an iterative process whereby various molecular structures are applied to said computer-generated model to identify potential agonists or antagonists to said peptide.
 74. The method of claim 73, wherein said substrate-binding site comprises amino acid residues 95 to 99, 155 to 168, 205 to 213, 215-217, and 257 to 261 of SEQ ID NO: 2 according to Table II.
 75. A method of assessing compounds which are agonists or antagonists of the activity of the human ERAB or HADH2 peptide comprising: (a) employing computational means to perform a fitting operation between the compounds and a substrate-binding site defined by crystallographic coordinates of amino acid residues 95 to 99, 155 to 168, 205 to 213, 215-217, and 257 to 261 of SEQ ID NO: 2 according to Table II; and (b) applying an iterative process whereby various molecular structures are applied to said fitting operation to identify potential agonists or antagonists to said peptide.
 76. The method of claim 75, wherein said substrate-binding site has amino acid residues selected from the group consisting of (a) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 2; (b) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 4; (c) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 6; (d) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 8; (e) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 20; and (f) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO:
 23. 77. A method of identifying a compound that associates with ERAB or HADH2, the method comprising the step of using the crystal coordinates of amino acid residues 95 to 99, 155 to 168, 205 to 213, 215-217, and 257 to 261 of SEQ ID NO: 2 according to Table II to computationally analyze a molecular structure to evaluate a chemical entity for associating with the substrate-binding site of ERAB or HADH2 and identifying those chemical entities that associate with said substrate-binding site, wherein said step of computationally analyzing the molecular structure comprises: (a) storing instructions for processing machine readable data wherein said data comprises crystal coordinates of amino acid residues 95 to 99, 155 to 168, 205 to 213, 215-217, and 257 to 261 of SEQ ID NO: 2 according to Table II; and (b) processing said data of crystal coordinates into a three-dimensional structure of said peptide molecule or complex.
 78. The method of claim 77 further comprising the step of displaying said crystal coordinates of the three-dimensional structure.
 79. A method of using a computer processor for analyzing a substrate-binding site of an ERAB or HADH2 peptide or ERAB or HADH2 peptide:NAD⁺:ligand complex comprising: (a) storing instructions for processing machine readable data wherein said data comprises X-ray crystallographic coordinates having crystal coordinates of amino acid residues 95 to 99, 155 to 168, 205 to 213, 215-217, and 257 to 261 of SEQ ID NO: 2 according to Table II; and p1 (b) processing said data of crystal coordinates into a three-dimensional structure of said peptide molecule or complex to analyze the substrate-binding site of said peptide.
 80. The method of claim 79 further comprising the step of displaying said crystal coordinates of the three-dimensional structure.
 81. The method of claim 79, wherein said ligand is an ERAB or HADH2 inhibitor.
 82. The method of claim 79, wherein said machine readable data storage medium is CD-ROM.
 83. The method of claim 79, wherein said machine readable data storage medium is a magneto-optic disk.
 84. A computer based method for processing X-ray coordinate data into a three-dimensional graphical display of a substrate-binding site of an ERAB or HADH2 peptide molecule or ERAB or HADH2 peptide:NAD⁺:ligand complex using the crystal coordinates of amino acid residues 95 to 99, 155 to 168, 205 to 213, 215-217, and 257 to 261 of SEQ ID NO: 2 according to Table II.
 85. The method of claim 84, wherein said ligand is an ERAB or HADH2 inhibitor.
 86. The method of claim 84, wherein said X-ray coordinate data is stored in a machine readable storage medium.
 87. The method of claim 84, wherein said three-dimensional graphical display is displayed on a computer monitor.
 88. A process of drug design for compounds which associate with a substrate-binding site of an ERAB or HADH2 peptide comprising: (a) employing computational means to perform a fitting operation between the compounds and a substrate-binding site defined by crystallographic coordinates of amino acid residues 95 to 99, 155 to 168, 205 to 213, 215-217, and 257 to 261 of SEQ ID NO: 2 according to Table II; and (b) applying an iterative process whereby various molecular structures are applied to said fitting operation to identify the compounds which associate with the substrate-binding site.
 89. The method of claim 88, wherein said substrate-binding site has amino acid residues selected from the group consisting of (a) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 2; (b) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 4; (c) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 6; (d) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 8; (e) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 20; and (f) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO:
 23. 90. The method of claim 73 or 79, wherein said substrate-binding site has amino acid residues selected from the group consisting of (a) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 2; (b) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 4; (c) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 6; (d) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 8; (e) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO: 20; and (f) residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO:
 23. 91. A method of identifying a compound that associates with an ERAB or HADH2 peptide, the method comprising using the crystal coordinates from Table II, or portions thereof, to computationally evaluate a chemical entity for associating with the substrate-binding site of ERAB or HADH2.
 92. A computer readable medium having stored thereon a model of a crystal structure comprising an ERAB or HADH2 peptide wherein said peptide has a substrate-binding site containing amino acid residues 95 to 99, 155 to 168, 205 to 217, and 257 to 261 of SEQ ID NO:
 2. 